[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. STRAIN=K12; PubMed=3286606 [NCBI, ExPASy, EBI, Israel, Japan] Cole S.T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W.F., Weiner J.H.; "Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12."; J. Bacteriol. 170:2448-2456(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/dnares/4.2.91; PubMed=9205837 [NCBI, ExPASy, EBI, Israel, Japan] Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."; DNA Res. 4:91-113(1997).
[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).

Comments

FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor.
COFACTOR: FAD.
COFACTOR: FMN.
PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route): step 1/1 .
SUBUNIT: Composed of a catalytic glpA/B dimer and of membrane bound glpC.
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. Note=Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase.
SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate 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

M20938; AAA83864.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75301.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA16060.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A32006; DEECNA.

RefSeq

AP_002838.1; -.
NP_416744.1; -.

3D structure databases

ModBase

P0A9C0.

Enzyme and pathway databases

BioCyc

EcoCyc:ANGLYC3PDEHYDROGSUBUNITA-MON; -.
MetaCyc:ANGLYC3PDEHYDROGSUBUNITA-MON; -.

Organism-specific databases

EchoBASE

EB0386; -.

EcoGene

EG10391; glpA.

Ontologies

GO:0009331;	Cellular component: glycerol-3-phosphate dehydrogenase complex (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004368;	Molecular function: glycerol-3-phosphate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0006072;	Biological process: glycerol-3-phosphate metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR017752; Anaerobic_glycerol3P_DH_asu.
IPR007419; BFD_Fer2_bd.
IPR000447; FAD-dep_Gly3P_DHase.
IPR006076; FAD-dep_OxRdtase.
Graphical view of domain structure.

Pfam

PF01266; DAO; 1.
PF04324; Fer2_BFD; 1.
Pfam graphical view of domain structure.

PRINTS

PR01001; FADG3PDH.

PROSITE

PS00977; FAD_G3PDH_1; 1.
PS00978; FAD_G3PDH_2; 1.

Genome annotation databases

GeneID

946713; -.

GenomeReviews

AP009048_GR; JW2235.
U00096_GR; b2241.

KEGG

ecj:JW2235; -.
eco:b2241; -.

Phylogenomic databases

HOGENOM

P0A9C0; -.

Genome annotation databases

CMR

P0A9C0; b2241.

Other

ProtoNet

P0A9C0.

UniRef

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

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Membrane; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 542`	`542`	`Anaerobic glycerol-3-phosphate dehydrogenase subunit A.`	`PRO_0000126093`
`NP_BIND`	`10 38`	`29`	`FAD (Potential).`
`CONFLICT`	`329 329`		`V -> L (in Ref. 1; AAA83864).`

Sequence information

Length: 542 AA [This is the length of the unprocessed precursor]

Molecular weight: 58958 Da [This is the MW of the unprocessed precursor]

CRC64: E5C803F89E912E0E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTRDSQSSD VIIIGGGATG AGIARDCALR GLRVILVERH DIATGATGRN HGLLHSGARY 

        70         80         90        100        110        120 
AVTDAESARE CISENQILKR IARHCVEPTN GLFITLPEDD LSFQATFIRA CEEAGISAEA 

       130        140        150        160        170        180 
IDPQQARIIE PAVNPALIGA VKVPDGTVDP FRLTAANMLD AKEHGAVILT AHEVTGLIRE 

       190        200        210        220        230        240 
GATVCGVRVR NHLTGETQAL HAPVVVNAAG IWGQHIAEYA DLRIRMFPAK GSLLIMDHRI 

       250        260        270        280        290        300 
NQHVINRCRK PSDADILVPG DTISLIGTTS LRIDYNEIDD NRVTAEEVDI LLREGEKLAP 

       310        320        330        340        350        360 
VMAKTRILRA YSGVRPLVAS DDDPSGRNVS RGIVLLDHAE RDGLDGFITI TGGKLMTYRL 

       370        380        390        400        410        420 
MAEWATDAVC RKLGNTRPCT TADLALPGSQ EPAEVTLRKV ISLPAPLRGS AVYRHGDRTP 

       430        440        450        460        470        480 
AWLSEGRLHR SLVCECEAVT AGEVQYAVEN LNVNSLLDLR RRTRVGMGTC QGELCACRAA 

       490        500        510        520        530        540 
GLLQRFNVTT SAQSIEQLST FLNERWKGVQ PIAWGDALRE SEFTRWVYQG LCGLEKEQKD 


AL

P0A9C0 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