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

From

Rhizobium meliloti (Sinorhizobium meliloti)

[TaxID: 382]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=GR4; PubMed=9004223 [NCBI, ExPASy, EBI, Israel, Japan] Jimenez-Zurdo J.I., Garcia-Rodriguez F.M., Toro N.; "The Rhizobium meliloti putA gene: its role in the establishment of the symbiotic interaction with alfalfa."; Mol. Microbiol. 23:85-93(1997).
[2]	AUTOREGULATORY ROLE. DOI=10.1128/JB.182.7.1935-1941.2000; PubMed=10715000 [NCBI, ExPASy, EBI, Israel, Japan] Soto M.J., Jimenez-Zurdo J.I., van Dillewijn P., Toro N.; "Sinorhizobium meliloti putA gene regulation: a new model within the family rhizobiaceae."; J. Bacteriol. 182:1935-1941(2000).

Comments

FUNCTION: Oxidizes proline to glutamate for use as a carbon and nitrogen source, and also functions as a transcriptional repressor of its own gene.
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 .
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

Y08500; CAA69727.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T43218; T43218.

3D structure databases

HSSP

P09546; 1K87. [HSSP ENTRY / PDB]

ModBase

P95629.

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.

Other

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

Keywords

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 1224`	`1224`	`Bifunctional protein putA.`	`PRO_0000056527`
`REGION`	`164 501`	`338`	`Proline dehydrogenase.`
`REGION`	`576 1032`	`457`	`Aldehyde dehydrogenase.`
`ACT_SITE`	`800 800`		`By similarity.`
`ACT_SITE`	`834 834`		`By similarity.`

Sequence information

Length: 1224 AA [This is the length of the unprocessed precursor]

Molecular weight: 131191 Da [This is the MW of the unprocessed precursor]

CRC64: BEC655494FCE98D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSPNPLQKPA IDAAPAPFAD FAPPVRPQST LRRAITAAYR RPETECLPPL VEAATQSKEI 

        70         80         90        100        110        120 
RDAAASTARK LIEALRGKHS GSGVEGLVQE YSLSSQEGVA LMCLAERPVR IPDTATRDAL 

       130        140        150        160        170        180 
IRDKIADGNW KSHLGRSRSL FVNAATWGLV VTGKLTSTVN DRTLAARVTR LISRCGEPVI 

       190        200        210        220        230        240 
RRGVDMAMRM MGEQFVTGET IEALKRSKEL EEKGFSYSYD MLRERPTAAD AERYYRDYES 

       250        260        270        280        290        300 
AIHATAKPRG RGIYEGPGIS IKLSALHPRY RQAARVMGEL LPRVKALALL AKNYDIGLNI 

       310        320        330        340        350        360 
DAEEADRLEL SLDLLEVLCL DGDLSGWNGM GFVVQAYGKR CPFVLDFIID LARRSGRRIM 

       370        380        390        400        410        420 
VRLVKGAYWD AEIKRAQLDG LADFPVFTRK IHTDVSYMPR TQAACRDRCG VPQFATHNAQ 

       430        440        450        460        470        480 
TLAAIYHMAG KDFHVGKYEF QCLHGMGEPL YEEVVGRGKL DRPCRIYAPV GTHETLLAYL 

       490        500        510        520        530        540 
VRRLLENGAN SSFVHRINDP KVSIDELIAD PVEVVRAMPV VGAKHDRIAL PAVLFGDART 

       550        560        570        580        590        600 
NSAGFDLSNE ETLASLTEAL RESAAMKWTA LPQFATGPAA GETRTVLNPG DHRDVVGSVT 

       610        620        630        640        650        660 
ETRKRTHGAP CACRRRGAGL GGRLAERAAC LDRAAELMQA RMPTLLGLII REAGKSALNA 

       670        680        690        700        710        720 
IAEVREAIDF LRYYAEQTRR TLGPATPLGP IVCISPWNFP LAIFTGQIAA ALVAGNPVLA 

       730        740        750        760        770        780 
KPAEETPLIA AEGVRILREA GIPASALQLL PGDGRVGAAL VAGRDAGVMF TGSTEVARLI 

       790        800        810        820        830        840 
QAQLADRLSP AGRPVPLIAE TGGQNAMIVD SSALAGQVVG DVITSAFDSA GQRCSALRVL 

       850        860        870        880        890        900 
CLQEDVAGPH PDDAEGRAAR HCISAAPIVF SVDVGPVITS EAKDNIEKHI ERMRGLGRKV 

       910        920        930        940        950        960 
EQIGLASETG VGTFVPPTII ELEKLSDLQR EVFGPVLHVI RYRRDDLDRL VDDVNATGYG 

       970        980        990       1000       1010       1020 
LTFGLHTRLD ETIAHVTSRI KAGNLYINRN IIGAVVGVQP FGGRGLSGTG PKAGGPLYLG 

      1030       1040       1050       1060       1070       1080 
RLVTTAPVPP QHSSVHTDPV LLDFAKWLDG KGARAEVEAA RNAGSSSALG LDLELPGPVG 

      1090       1100       1110       1120       1130       1140 
ERNLYTLHAR GRILLVPATE SGLYHQLAAA LATGNSVAID AASGLQASLK NLPQTVGLRV 

      1150       1160       1170       1180       1190       1200 
SWSKDWAADG PFAGALVEGD AERIRAVNKA IAALPGPLLL VQAASSGEIA RNPDAYCLNW 

      1210       1220 
LVEEVSASIN TAAAGGNASL MAIG

P95629 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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