Reviewed, UniProtKB/Swiss-Prot P0C8Z1 (G3P1_ESCFE)

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

Organism

Escherichia fergusonii

Taxonomic identifier

564 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	294 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (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 – ›294	›294	Glyceraldehyde-3-phosphate dehydrogenase A		PRO_0000145657
Regions
	Region	134 – 136	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	194 – 195	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	135	1	Nucleophile By similarity
	Binding site	19	1	NAD By similarity
	Binding site	63	1	NAD; via carbonyl oxygen By similarity
	Binding site	165	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	217	1	Glyceraldehyde 3-phosphate By similarity
	Site	162	1	Activates thiol group during catalysis By similarity
Natural variations
	Natural variant	153	1	I → M in strain: ATCC 35471.
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	294	1

Sequences

	Sequence		Length	Mass (Da)
	P0C8Z1-1 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 2A93A1824586F029	FASTA	294	31,404
	10 20 30 40 50 60 IVFRAAQKRS DIEIVAINDL LDADYMAYML KYDSTHGRFD GTVEVKDGHL IVNGKKIRVT 70 80 90 100 110 120 AERDPANLKW DEVGVDVVAE ATGIFLTDET ARKHITAGAK KVVLTGPSKD NTPMFVKGAN 130 140 150 160 170 180 FDKYAGQDIV SNASCTTNCL APLAKVINDN FGIIEGLMTT VHATTATQKT VDGPSHKDWR 190 200 210 220 230 240 GGRGASQNII PSSTGAAKAV GKVLPELNGK LTGMAFRVPT PNVSVVDLTV RLEKPATYEQ 250 260 270 280 290 IKAAVKAAAE GEMKGVLGYT EDDVVSTDFN GEVCTSVFDA KAGIALNDNF VKLV

References

[1]	"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]. Strain: ATCC 35471 / CDC 1016-74 and ATCC 35472 / CDC 3014-74.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M63367 Genomic DNA. Translation: AAA23424.1. M63368 Genomic DNA. Translation: AAA23425.1.
PIR	I41118. I41119.
3D structure databases
HSSP	HSSP built from PDB template 1DC5 based on UniProtKB P06977.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.12. 290708.
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_1. [Graphical view]
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.
TIGRFAMs	TIGR01534. GAPDH-I. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P1_ESCFE

Accession

Primary (citable) accession number: P0C8Z1
Secondary accession number(s): P24746

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 24, 2009
Last modified:	June 16, 2009
This is version 3 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)