P0A9C0 (GLPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

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:	b2241, JW2235

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	542 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor.
Catalytic activity	sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
Cofactor	FAD. FMN.
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.
Subcellular location	Cell inner membrane; Peripheral membrane protein. Note: Loosely bound to the cytoplasmic membrane often occurring in vesicles associated with fumarate reductase.
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glycerol catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glycerol-3-phosphate metabolic 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	FMN binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro sn-glycerol-3-phosphate:ubiquinone-8 oxidoreductase activity Inferred from electronic annotation. Source: EC
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_0000126093
Regions
	Nucleotide binding	10 – 38	29	FAD Potential
Experimental info
	Sequence conflict	329	1	V → L in AAA83864. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0A9C0 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and gene-polypeptide relationships of the glpABC operon encoding the anaerobic sn-glycerol-3-phosphate dehydrogenase of Escherichia coli K-12." Cole S.T., Eiglmeier K., Ahmed S., Honore N., Elmes L., Anderson W.F., Weiner J.H. J. Bacteriol. 170:2448-2456(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: K12.
[2]	"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." 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. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M20938 Genomic DNA. Translation: AAA83864.1. U00096 Genomic DNA. Translation: AAC75301.1. AP009048 Genomic DNA. Translation: BAA16060.1.
PIR	DEECNA. A32006.
RefSeq	NP_416744.1. NC_000913.2. YP_490480.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A9C0.
SMR	P0A9C0. Positions 8-365.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A9C0. 4 interactions.
STRING	511145.b2241.
Proteomic databases
PaxDb	P0A9C0.
PRIDE	P0A9C0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75301; AAC75301; b2241. BAA16060; BAA16060; BAA16060.
GeneID	12930620. 946713.
KEGG	ecj:Y75_p2203. eco:b2241.
PATRIC	32119841. VBIEscCol129921_2330.
Organism-specific databases
EchoBASE	EB0386.
EcoGene	EG10391. glpA.
Phylogenomic databases
eggNOG	COG0578.
HOGENOM	HOG000004814.
KO	K00111.
OMA	VRVFDHK.
ProtClustDB	PRK11101.
Enzyme and pathway databases
BioCyc	EcoCyc:ANGLYC3PDEHYDROGSUBUNITA-MONOMER. ECOL316407:JW2235-MONOMER. MetaCyc:ANGLYC3PDEHYDROGSUBUNITA-MONOMER.
UniPathway	UPA00618; UER00673.
Gene expression databases
Genevestigator	P0A9C0.
Family and domain databases
InterPro	IPR007419. BFD-like_2Fe2S-bd_dom. IPR006076. FAD-dep_OxRdtase. IPR000447. G3P_DH_FAD-dep. IPR017752. G3P_DH_GlpA_su. [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_ECOLI

Accession

Primary (citable) accession number: P0A9C0
Secondary accession number(s): P13032, P78238

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program