Reviewed, UniProtKB/Swiss-Prot P34916 (G3P1_ANAVT)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 1
    EC=1.2.1.12

Gene names

Name:	gap1
Ordered Locus Names:	Ava_0495

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 343	342	Glyceraldehyde-3-phosphate dehydrogenase 1		PRO_0000145624
Regions
	Nucleotide binding	13 – 14	2	NAD By similarity
	Region	154 – 156	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	214 – 215	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	155	1	Nucleophile By similarity
	Binding site	35	1	NAD By similarity
	Binding site	79	1	NAD; via carbonyl oxygen By similarity
	Binding site	185	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	237	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	319	1	NAD By similarity
	Site	182	1	Activates thiol group during catalysis By similarity
Experimental info
	Sequence conflict	240	1	T → I in AAA21995. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P34916-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 307D0703DF8D279C	FASTA	343	36,666
	10 20 30 40 50 60 MAKLKVGING FGRIGRLVLR AGINNPNIEF VGINDLVPPD NLAYLLKYDS THGKLRSQVE 70 80 90 100 110 120 AKDDGIVIDG HFIPCVSVRN PAELPWGKLG ADYVVESTGL FTDSEGASKH LQAGAKRVII 130 140 150 160 170 180 SAPTKDPDRV RTLLVGVNHD LFDPSKDVIV SNASCTTNCL APIAKVINDN FGLTEGLMTT 190 200 210 220 230 240 VHAMTATQPT VDGPSKKDWR GGRGAAQNII PSSTGAAKAV ALVLPELKGK LTGMAFRVPT 250 260 270 280 290 300 PDVSVVDLTF KTAKATSYKE ICAAMKQASE GSLAGILGYT DEEVVSTDFQ GDTHSSIFDA 310 320 330 340 GAGIELNSNF FKVVAWYDNE WGYSNRVVDL MLSMIQKEQL AAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for a chimeric nature of nuclear genomes: eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes." Martin W., Brinkmann H., Savona C., Cerff R. Proc. Natl. Acad. Sci. U.S.A. 90:8692-8696(1993) [PubMed: 8378350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L07497 Genomic DNA. Translation: AAA21995.2. CP000117 Genomic DNA. Translation: ABA20119.1.
PIR	I39602.
RefSeq	YP_321014.1.
3D structure databases
HSSP	HSSP built from PDB template 1DC5 based on UniProtKB P06977.
ModBase	Search...
Genome annotation databases
GeneID	3682402.
GenomeReviews	Gene locus Ava_0495 in contig CP000117_GR.
KEGG	ava:Ava_0495.
NMPDR	fig|240292.3.peg.1853.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P34916.
OMA	P34916. KEICTEV.
Enzyme and pathway databases
BioCyc	AVAR240292:AVA_0495-MON.
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_ANAVT

Accession

Primary (citable) accession number: P34916
Secondary accession number(s): Q3MFW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 69 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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