Reviewed, UniProtKB/Swiss-Prot P58559 (G3P3_ANASP)

Names and origin

Protein names

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

Gene names

Name:	gap3
Ordered Locus Names:	alr1095

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 transcript 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 heterocysts. Ref.2
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
	Chain	1 – 337	337	Glyceraldehyde-3-phosphate dehydrogenase 3		PRO_0000145627
Regions
	Nucleotide binding	12 – 13	2	NAD By similarity
	Region	152 – 154	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	211 – 212	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	153	1	Nucleophile By similarity
	Binding site	183	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	198	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	234	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	317	1	NAD By similarity
	Site	180	1	Activates thiol group during catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58559-1 [UniParc]. Last modified January 23, 2002. Version 1. Checksum: F86B22C5BCAD32AF	FASTA	337	37,117
	10 20 30 40 50 60 MKVRVGINGF GRMGRLALRA AWDWPELEFV HINEIKGGAV AAAHLLKFDS VHGRWTPEVE 70 80 90 100 110 120 AEGERVLIDG TPLSFSEYGK PDDVPWEDFG VDLVLECSGK FRTPATLDPY FKRGVQKVIV 130 140 150 160 170 180 AAPVKEEALN IVMGVNDYLY EPEKHHLLTA ASCTTNCLAP VVKVIHEGLG IKHGIITTIH 190 200 210 220 230 240 DNTNTQTLVD APHKDLRRAR ATSLSLIPTT TGSATAIALI YPELKGKLNG IAVRVPLLNA 250 260 270 280 290 300 SLTDCVFEVT RPTTVEEINA LLKAASEQAP LQGILGYEER PLVSIDYKDD PRSSIIDALS 310 320 330 TMVVDETQVK ILAWYDNEWG YVNRMVELAR KVALSLK

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: DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000019 Genomic DNA. Translation: BAB73052.1.
PIR	AD1943.
RefSeq	NP_485138.1.
3D structure databases
HSSP	HSSP built from PDB template 4DBV based on UniProtKB P00362.
ModBase	Search...
Genome annotation databases
GeneID	1104689.
GenomeReviews	Gene locus alr1095 in contig BA000019_GR.
KEGG	ana:alr1095.
NMPDR	fig|103690.1.peg.1405.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P58559.
OMA	P58559. VHINEIK.
Enzyme and pathway databases
BioCyc	NSP103690:ALR1095-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

G3P3_ANASP

Accession

Primary (citable) accession number: P58559

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	January 23, 2002
Last modified:	June 16, 2009
This is version 48 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)