Reviewed, UniProtKB/Swiss-Prot P0A9C1 (GLPA_ECO57)

Names and origin

Protein names

Recommended name:
    Anaerobic glycerol-3-phosphate dehydrogenase subunit A
      Short name=G-3-P dehydrogenase
    EC=1.1.5.3

Gene names

Name:	glpA
Ordered Locus Names:	Z3499, ECs3126

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor By similarity.
Catalytic activity	sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
Cofactor	FAD By similarity. 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 structure	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.
Sequence similarities	Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycerol-3-phosphate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW polyol catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	glycerol-3-phosphate dehydrogenase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro glycerol-3-phosphate dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 542	542	Anaerobic glycerol-3-phosphate dehydrogenase subunit A		PRO_0000126094
Regions
	Nucleotide binding	10 – 38	29	FAD Potential

Sequences

	Sequence		Length	Mass (Da)
	P0A9C1-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: E5C803F89E912E0E	FASTA	542	58,958
	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

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005174 Genomic DNA. Translation: AAG57372.1. BA000007 Genomic DNA. Translation: BAB36549.1.
PIR	F91019.
RefSeq	NP_288817.1. NP_311153.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	916834. 959442.
GenomeReviews	Gene locus Z3499 in contig AE005174_GR. Gene locus ECs3126 in contig BA000007_GR.
KEGG	ece:Z3499. ecs:ECs3126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A9C1.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3126-MON.
Family and domain databases
InterPro	IPR017752. Anaerobic_glycerol3P_DH_asu. IPR007419. BFD_Fer2_bd. IPR000447. FAD-dep_Gly3P_DH. IPR006076. FAD-dep_OxRdtase. [Graphical view]
Pfam	PF01266. DAO. 1 hit. PF04324. Fer2_BFD. 1 hit. [Graphical view]
PRINTS	PR01001. FADG3PDH.
TIGRFAMs	TIGR03377. glycerol3P_GlpA. 1 hit.
PROSITE	PS00977. FAD_G3PDH_1. 1 hit. PS00978. FAD_G3PDH_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLPA_ECO57

Accession

Primary (citable) accession number: P0A9C1
Secondary accession number(s): P13032, P78238

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)