NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=102F34;
PubMed=9141699 [NCBI, ExPASy, EBI, Israel, Japan]
Pocard J.A., Vincent N., Boncompagni E., Tombras Smith L., Poggi M.-C., Le Rudulier D.;
"Molecular characterization of the bet genes encoding glycine betaine synthesis in Sinorhizobium meliloti 102F34.";
Microbiology 143:1369-1379(1997).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1021;
DOI=10.1073/pnas.161294398; PubMed=11481430 [NCBI, ExPASy, EBI, Israel, Japan]
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.;
"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021.";
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).

Comments

FUNCTION: Can catalyze the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine (By similarity).
CATALYTIC ACTIVITY: Choline + acceptor = betaine aldehyde + reduced acceptor.
COFACTOR: FAD.
PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1 .
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
SIMILARITY: Belongs to the GMC oxidoreductase 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

U39940; AAC13369.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL591688; CAC45519.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_385053.1; -.

3D structure databases

ModBase

P54223.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-244; -.
SMEL266834:SMC00093-MON; -.

Ontologies

GO:0008812;	Molecular function: choline dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019285;	Biological process: glycine betaine biosynthetic process from choline (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00750; -; 1.
PBIL [Tree]

InterPro

IPR011533; Choline_dehydrogenase.
IPR012132; GMC_OxRdtase.
IPR000172; GMC_OxRdtase_N.
IPR007867; GMC_OxRtase_C.
Graphical view of domain structure.

Pfam

PF05199; GMC_oxred_C; 1.
PF00732; GMC_oxred_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000137; Alcohol_oxidase; 1.

TIGRFAMs

TIGR01810; betA; 1.

PROSITE

PS00623; GMC_OXRED_1; 1.
PS00624; GMC_OXRED_2; 1.

BLOCKS

P54223.

Genome annotation databases

1232590; -.

AL591688_GR; R00947.

sme:SMc00093; -.

fig|266834.1.peg.2241; -.

Phylogenomic databases

HOGENOM

P54223; -.

Genome annotation databases

CMR

P54223; R00947.

Other

ProtoNet

P54223.

UniRef

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

Keywords

Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 549`	`549`	`Choline dehydrogenase.`	`PRO_0000205594`
`NP_BIND`	`4 33`	`30`	`FAD (Probable).`
`ACT_SITE`	`465 465`		`By similarity.`
`CONFLICT`	`267 267`		`A -> R (in Ref. 1; AAC13369).`
`CONFLICT`	`417 424`		`RHCVRLTR -> DLRAVTG (in Ref. 1; AAC13369).`
`CONFLICT`	`429 429`		`Q -> E (in Ref. 1; AAC13369).`

Sequence information

Length: 549 AA [This is the length of the unprocessed precursor]

Molecular weight: 61291 Da [This is the MW of the unprocessed precursor]

CRC64: 29BE064F40CB88F4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQADFVIIGS GSAGSALAYR LSEDGRNSVI VLEFGGSDVG PFIQMPAALA WPMSMNRYNW 

        70         80         90        100        110        120 
GYLSEPEPNL NNRRITAPRG KVIGGSSSIN GMVYVRGHSE DFNRWEELGA QGWAYADVLP 

       130        140        150        160        170        180 
YYKRMEHSHG GEEGWRGTDG PLHVQRGPVK NPLFHAFIEA GKEAGFEVTE DYNGSKQEGF 

       190        200        210        220        230        240 
GLMEQTTWRG RRWSAASAYL RPALKRPNVE LIRCFARKIV IENGRATGVE IERGGRIEVV 

       250        260        270        280        290        300 
KANREVIVSA SSFNSPKLLM LSGIGPAAHL KEMGIDVKVD RPGVGQNLQD HMEFYFQQVS 

       310        320        330        340        350        360 
TKPVSLYSWL PWFWQGVAGA QWLFFKRGLG ISNQFESCAF LRSAPGVKQP DIQYHFLPVA 

       370        380        390        400        410        420 
ISYDGKAAAK SHGFQVHVGY NLSKSRGNVS LRSSDPKADP VIRFNYMSHP EDWEKFRHCV 

       430        440        450        460        470        480 
RLTREIFGQK AFDLYRGPEI QPGEKVQTDE EIDGFLREHL ESAYHPCGTC KMGAKDDPMA 

       490        500        510        520        530        540 
VVDPETRVIG VDGLRVADSS IFPHITYGNL NAPSIMTGEK SADHILGRQP LARSNQEPWI 


NPRWAVSDR

P54223 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