Proline dehydrogenase
     (EC 1.5.99.8)
     (Proline oxidase)
Delta-1-pyrroline-5-carboxylate dehydrogenase
     (P5C dehydrogenase)
     (EC 1.5.1.12)

Gene name

	Name:	putA
	Synonyms:	poaA
	OrderedLocusNames:	b1014, JW0999

From

Escherichia coli (strain K12)

[TaxID: 83333]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1006/jmbi.1994.1696; PubMed=7966312 [NCBI, ExPASy, EBI, Israel, Japan] Ling M., Allen S.W., Wood J.M.; "Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein."; J. Mol. Biol. 243:950-956(1994).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan] Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.; "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."; DNA Res. 3:137-155(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60. STRAIN=K12; DOI=10.1007/BF00325707; PubMed=3325781 [NCBI, ExPASy, EBI, Israel, Japan] Nakao T., Yamato I., Anraku Y.; "Nucleotide sequence of putC, the regulatory region for the put regulon of Escherichia coli K12."; Mol. Gen. Genet. 210:364-368(1987).
[6]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-669 IN COMPLEX WITH FAD, AND HOMODIMERIZATION. DOI=10.1038/nsb885; PubMed=12514740 [NCBI, ExPASy, EBI, Israel, Japan] Lee Y.-H., Nadaraia S., Gu D., Becker D.F., Tanner J.J.; "Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein."; Nat. Struct. Biol. 10:109-114(2003).

Comments

FUNCTION: Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon.
CATALYTIC ACTIVITY: L-proline + acceptor + H₂O = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)⁺ + 2 H₂O = L-glutamate + NAD(P)H.
COFACTOR: FAD.
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2 .
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2 .
SUBUNIT: Homodimer.
INTERACTION:
P63389:yheS; NbExp=1; IntAct=EBI-369718, EBI-561198;
INDUCTION: By proline, autorepression and catabolite repression, and is potentially nitrogen controlled.
SIMILARITY: In the N-terminal section; belongs to the proline dehydrogenase family.
SIMILARITY: In the C-terminal section; belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U05212; AAB59985.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74099.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35791.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05653; CAA29141.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D64843; D64843.

RefSeq

AP_001645.1; -.
NP_415534.1; -.

3D structure databases

PDB

1K87; X-ray; 2.00 A; A=1-669.	[ExPASy / RCSB / EBI]
1TIW; X-ray; 2.00 A; A=86-669.	[ExPASy / RCSB / EBI]
1TJ0; X-ray; 2.10 A; A=86-669.	[ExPASy / RCSB / EBI]
1TJ1; X-ray; 2.00 A; A=86-669.	[ExPASy / RCSB / EBI]
1TJ2; X-ray; 2.05 A; A=86-669.	[ExPASy / RCSB / EBI]
2AY0; X-ray; 2.10 A; A/B/C/D/E/F=1-52.	[ExPASy / RCSB / EBI]
2FZM; X-ray; 2.30 A; A=86-673.	[ExPASy / RCSB / EBI]
2FZN; X-ray; 2.00 A; A=86-673.	[ExPASy / RCSB / EBI]
2GPE; X-ray; 1.90 A; A/B/C/D=1-52.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1K87; -.
1TIW; -.
1TJ0; -.
1TJ1; -.
1TJ2; -.
2AY0; -.
2FZM; -.
2FZN; -.
2GPE; -.

ModBase

P09546.

Protein-protein interaction databases

DIP

DIP:10620N; -.

IntAct

P09546; -.

Enzyme and pathway databases

BioCyc

EcoCyc:PUTA-MON; -.

Organism-specific databases

EchoBASE

EB0794; -.

EcoGene

EG10801; putA.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR005933; d-1-pyrroline-5-COlate_DHase-3.
IPR002872; Proline_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
PF01619; Pro_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01238; D1pyr5carbox3; 1.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

BLOCKS

P09546.

Genome annotation databases

GeneID

945600; -.

GenomeReviews

U00096_GR; b1014.
AP009048_GR; JW0999.

KEGG

ecj:JW0999; -.
eco:b1014; -.

Phylogenomic databases

HOGENOM

P09546; -.

Genome annotation databases

CMR

P09546; b1014.

Other

ProtoNet

P09546.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; DNA-binding; FAD; Flavoprotein; Multifunctional enzyme; NAD; Oxidoreductase; Proline metabolism; Repressor; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1320`	`1320`	`Bifunctional protein putA.`	`PRO_0000056524`
`REGION`	`228 574`	`347`	`Proline dehydrogenase.`
`REGION`	`653 1119`	`467`	`Aldehyde dehydrogenase.`
`ACT_SITE`	`883 883`		`By similarity.`
`ACT_SITE`	`917 917`		`By similarity.`
`CONFLICT`	`531 531`		`G -> A (in Ref. 1; AAB59985).`
`HELIX`	`90 97`	`8`
`TURN`	`98 100`	`3`
`HELIX`	`103 114`	`12`
`HELIX`	`118 136`	`19`
`TURN`	`137 140`	`4`
`HELIX`	`141 153`	`13`
`TURN`	`154 156`	`3`
`HELIX`	`161 173`	`13`
`HELIX`	`178 187`	`10`
`TURN`	`188 192`	`5`
`TURN`	`203 206`	`4`
`HELIX`	`210 214`	`5`
`HELIX`	`225 235`	`11`
`TURN`	`236 239`	`4`
`HELIX`	`241 256`	`16`
`HELIX`	`257 259`	`3`
`STRAND`	`261 264`	`4`
`HELIX`	`265 276`	`12`
`TURN`	`277 279`	`3`
`STRAND`	`281 286`	`6`
`HELIX`	`294 315`	`22`
`HELIX`	`319 322`	`4`
`STRAND`	`325 328`	`4`
`HELIX`	`330 332`	`3`
`HELIX`	`337 339`	`3`
`HELIX`	`342 363`	`22`
`STRAND`	`367 369`	`3`
`HELIX`	`374 376`	`3`
`HELIX`	`377 387`	`11`
`HELIX`	`391 393`	`3`
`STRAND`	`399 404`	`6`
`HELIX`	`410 423`	`14`
`STRAND`	`428 433`	`6`
`HELIX`	`438 448`	`11`
`HELIX`	`459 474`	`16`
`TURN`	`477 479`	`3`
`STRAND`	`480 485`	`6`
`HELIX`	`489 498`	`10`
`HELIX`	`505 507`	`3`
`STRAND`	`509 513`	`5`
`TURN`	`514 516`	`3`
`HELIX`	`518 521`	`4`
`TURN`	`522 524`	`3`
`HELIX`	`528 530`	`3`
`STRAND`	`537 543`	`7`
`HELIX`	`546 548`	`3`
`HELIX`	`550 561`	`12`
`HELIX`	`566 569`	`4`
`HELIX`	`577 580`	`4`
`HELIX`	`584 595`	`12`
`STRAND`	`596 599`	`4`

Sequence information

Length: 1320 AA [This is the length of the unprocessed precursor]

Molecular weight: 143815 Da [This is the MW of the unprocessed precursor]

CRC64: E4920143D536F7F9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGTTTMGVKL DDATRERIKS AATRIDRTPH WLIKQAIFSY LEQLENSDTL PELPALLSGA 

        70         80         90        100        110        120 
ANESDEAPTP AEEPHQPFLD FAEQILPQSV SRAAITAAYR RPETEAVSML LEQARLPQPV 

       130        140        150        160        170        180 
AEQAHKLAYQ LADKLRNQKN ASGRAGMVQG LLQEFSLSSQ EGVALMCLAE ALLRIPDKAT 

       190        200        210        220        230        240 
RDALIRDKIS NGNWQSHIGR SPSLFVNAAT WGLLFTGKLV STHNEASLSR SLNRIIGKSG 

       250        260        270        280        290        300 
EPLIRKGVDM AMRLMGEQFV TGETIAEALA NARKLEEKGF RYSYDMLGEA ALTAADAQAY 

       310        320        330        340        350        360 
MVSYQQAIHA IGKASNGRGI YEGPGISIKL SALHPRYSRA QYDRVMEELY PRLKSLTLLA 

       370        380        390        400        410        420 
RQYDIGINID AEESDRLEIS LDLLEKLCFE PELAGWNGIG FVIQAYQKRC PLVIDYLIDL 

       430        440        450        460        470        480 
ATRSRRRLMI RLVKGAYWDS EIKRAQMDGL EGYPVYTRKV YTDVSYLACA KKLLAVPNLI 

       490        500        510        520        530        540 
YPQFATHNAH TLAAIYQLAG QNYYPGQYEF QCLHGMGEPL YEQVTGKVAD GKLNRPCRIY 

       550        560        570        580        590        600 
APVGTHETLL AYLVRRLLEN GANTSFVNRI ADTSLPLDEL VADPVTAVEK LAQQEGQTGL 

       610        620        630        640        650        660 
PHPKIPLPRD LYGHGRDNSA GLDLANEHRL ASLSSALLNS ALQKWQALPM LEQPVAAGEM 

       670        680        690        700        710        720 
SPVINPAEPK DIVGYVREAT PREVEQALES AVNNAPIWFA TPPAERAAIL HRAAVLMESQ 

       730        740        750        760        770        780 
MQQLIGILVR EAGKTFSNAI AEVREAVDFL HYYAGQVRDD FANETHRPLG PVVCISPWNF 

       790        800        810        820        830        840 
PLAIFTGQIA AALAAGNSVL AKPAEQTPLI AAQGIAILLE AGVPPGVVQL LPGRGETVGA 

       850        860        870        880        890        900 
QLTGDDRVRG VMFTGSTEVA TLLQRNIASR LDAQGRPIPL IAETGGMNAM IVDSSALTEQ 

       910        920        930        940        950        960 
VVVDVLASAF DSAGQRCSAL RVLCLQDEIA DHTLKMLRGA MAECRMGNPG RLTTDIGPVI 

       970        980        990       1000       1010       1020 
DSEAKANIER HIQTMRSKGR PVFQAVRENS EDAREWQSGT FVAPTLIELD DFAELQKEVF 

      1030       1040       1050       1060       1070       1080 
GPVLHVVRYN RNQLPELIEQ INASGYGLTL GVHTRIDETI AQVTGSAHVG NLYVNRNMVG 

      1090       1100       1110       1120       1130       1140 
AVVGVQPFGG EGLSGTGPKA GGPLYLYRLL ANRPESALAV TLARQDAKYP VDAQLKAALT 

      1150       1160       1170       1180       1190       1200 
QPLNALREWA ANRPELQALC TQYGELAQAG TQRLLPGPTG ERNTWTLLPR ERVLCIADDE 

      1210       1220       1230       1240       1250       1260 
QDALTQLAAV LAVGSQVLWP DDALHRQLVK ALPSAVSERI QLAKAENITA QPFDAVIFHG 

      1270       1280       1290       1300       1310       1320 
DSDQLRALCE AVAARDGTIV SVQGFARGES NILLERLYIE RSLSVNTAAA GGNASLMTIG

P09546 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools