NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor (By similarity).
CATALYTIC ACTIVITY: sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor.
COFACTOR: FAD (By similarity).
COFACTOR: FMN (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein (By similarity). Note=Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase (By similarity).
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

AE005674; AAN43838.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP17656.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_708131.2; -.
NP_837846.1; -.

3D structure databases

ModBase

P0A9C2.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN43838.1-MON; -.

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

1025493; -.
1078747; -.

GenomeReviews

AE005674_GR; SF2323.
AE014073_GR; S2456.

KEGG

sfl:SF2323; -.
sfx:S2456; -.

Phylogenomic databases

HOGENOM

P0A9C2; -.

Genome annotation databases

CMR

P0A9C2; SF2323.

Other

ProtoNet

P0A9C2.

UniRef

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

Keywords

Cell inner membrane; Cell membrane; Complete proteome; 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_0000126096`
`NP_BIND`	`10 38`	`29`	`FAD (Potential).`

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

P0A9C2 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