Reviewed, UniProtKB/Swiss-Prot P58554 (G3P2_ANASP)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
    EC=1.2.1.12

Gene names

Name:	gap2
Ordered Locus Names:	all5062

Organism

Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 By similarity.
Subcellular location	Cytoplasm.
Developmental stage	Expressed in vegetative cells and heterocysts, expression is higher in vegetative cells. Ref.2
Sequence similarities	Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.
Mass spectrometry	Molecular mass is 37115 Da from positions 1 - 337. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
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 – 337	337	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145625
Regions
	Nucleotide binding	11 – 12	2	NAD By similarity
	Region	153 – 155	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	212 – 213	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	154	1	Nucleophile By similarity
	Binding site	35	1	NAD By similarity
	Binding site	80	1	NAD; via carbonyl oxygen By similarity
	Binding site	184	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	199	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	235	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	317	1	NAD By similarity
	Site	181	1	Activates thiol group during catalysis By similarity
Experimental info
	Sequence conflict	252	1	K → N in CAC41001. Ref.2
	Sequence conflict	319	1	W → C in CAC41001. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P58554-1 [UniParc]. Last modified January 23, 2002. Version 1. Checksum: 6671C88D5CC7E033	FASTA	337	36,910
	10 20 30 40 50 60 MIRVAINGFG RIGRNFARCW LGRENTNIEL VAVNDTSDPR TNAHLLKYDS MLGKLKNVDI 70 80 90 100 110 120 TADDNSITVN GKTIKCVSDR NPENLPWKEW EIDLIIEATG VFVSKEGATK HINAGAKKVL 130 140 150 160 170 180 ITAPGKNEDG TFVMGVNHHD YDHNLHNIIS NASCTTNCLA PIAKVLNDKF GIIKGSMTTT 190 200 210 220 230 240 HSYTGDQRLL DASHRDLRRA RAAAINIVPT STGAAKAVAL VIPELKGKLN GVALRVPTPN 250 260 270 280 290 300 VSMVDFVVQV EKRTITEEVN QALKDASEGP LKGILDYSEL QLVSSDYQGT DASSIVDANL 310 320 330 TLVMGNDLVK VMAWYDNEWG YSQRVLDLAE LVAEKWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Simultaneous occurrence of two different glyceraldehyde-3-phosphate dehydrogenases in heterocystous N(2)-fixing cyanobacteria." Valverde F., Peleato M.L., Fillat M.F., Gomez-Moreno C., Losada M., Serrano A. Biochem. Biophys. Res. Commun. 283:356-363(2001) [PubMed: 11327708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-320, DEVELOPMENTAL STAGE.
[3]	Singh H., Rajaram H., Apte S.K. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 265-272, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000019 Genomic DNA. Translation: BAB76761.1. AJ251774 Genomic DNA. Translation: CAC41001.1.
PIR	AF2438.
RefSeq	NP_489102.1.
3D structure databases
HSSP	HSSP built from PDB template 1NBO based on UniProtKB P19866.
SMR	P58554. Positions 2-335.
ModBase	Search...
Protein-protein interaction databases
STRING	P58554.
Genome annotation databases
GeneID	1108666.
GenomeReviews	Gene locus all5062 in contig BA000019_GR.
KEGG	ana:all5062.
NMPDR	fig|103690.1.peg.5369.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P58554.
OMA	NTDEKAS.
Enzyme and pathway databases
BioCyc	NSP103690:ALL5062-MON.
Family and domain databases
InterPro	IPR000173. GlycerAld_3-P_DH. IPR006424. Glyceraldehyde-3-P_DH_1. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.
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

G3P2_ANASP

Accession

Primary (citable) accession number: P58554
Secondary accession number(s): Q93M82

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2002
Last modified:	November 3, 2009
This is version 52 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)