B7LQ20 (G3P1_ESCF3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glyceraldehyde-3-phosphate dehydrogenase A
Short name=GAPDH-A
EC=1.2.1.12

Gene names

Name:	gapA
Synonyms:	gap
Ordered Locus Names:	EFER_1293

Organism

Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) [Complete proteome] [HAMAP]

Taxonomic identifier

585054 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) 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 – 331	331	Glyceraldehyde-3-phosphate dehydrogenase A		PRO_0000367318
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	149 – 151	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	209 – 210	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	150	1	Nucleophile By similarity
	Binding site	34	1	NAD By similarity
	Binding site	78	1	NAD; via carbonyl oxygen By similarity
	Binding site	180	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	232	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	314	1	NAD By similarity
	Site	177	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7LQ20 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 746397A4D815DCDE	FASTA	331	35,540
	10 20 30 40 50 60 MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST HGRFDGTVEV 70 80 90 100 110 120 KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGIF LTDETARKHI TAGAKKVVLT 130 140 150 160 170 180 GPSKDNTPMF VKGANFDKYA GQDIVSNASC TTNCLAPLAK VINDNFGIIE GLMTTVHATT 190 200 210 220 230 240 ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV 250 260 270 280 290 300 VDLTVRLEKP ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA 310 320 330 LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35469 / DSM 13698 / CDC 0568-73.
[2]	"Molecular and evolutionary relationships among enteric bacteria." Lawrence J.G., Ochman H., Hartl D.L. J. Gen. Microbiol. 137:1911-1921(1991) [PubMed: 1955870] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-309.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928158 Genomic DNA. Translation: CAQ88817.1. M63366 Genomic DNA. Translation: AAA23423.1.
RefSeq	YP_002382450.1. NC_011740.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B7LQ20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000122712; EBESCP00000114864; EBESCG00000124472.
GeneID	7123525.
GenomeReviews	Gene locus EFER_1293 in contig CU928158_GR.
KEGG	efe:EFER_1293.
PATRIC	32126981. VBIEscFer122920_1247.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009772.
HOGENOM	HBG571736.
ProtClustDB	PRK15425.
Enzyme and pathway databases
BioCyc	EFER585054:EFER_1293-MONOMER.
Family and domain databases
InterPro	IPR020831. GlycerAld/Erythrose_P_DH. IPR020830. GlycerAld_3-P_DH_AS. IPR020829. GlycerAld_3-P_DH_cat. IPR020828. GlycerAld_3-P_DH_NAD(P)-bd. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00134.
PANTHER	PTHR10836. GAP_DH. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
PRINTS	PR00078. G3PDHDRGNASE.
SMART	SM00846. Gp_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P1_ESCF3

Accession

Primary (citable) accession number: B7LQ20
Secondary accession number(s): P24746

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program