Reviewed, UniProtKB/Swiss-Prot P58838 (G3P2_METAC)

Names and origin

Protein names

Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase 2
      Short name=GAPDH 2
    EC=1.2.1.59
Alternative name(s):
    NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase 2

Gene names

Name:	gapB
Ordered Locus Names:	MA_3345

Organism

Methanosarcina acetivorans [Complete proteome] [HAMAP]

Taxonomic identifier

2214 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity Inferred from electronic annotation. Source: EC glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 335	335	Glyceraldehyde-3-phosphate dehydrogenase 2		PRO_0000145719
Regions
	Nucleotide binding	13 – 14	2	NAD By similarity
	Region	140 – 142	3	Glyceraldehyde 3-phosphate binding By similarity
	Region	195 – 196	2	Glyceraldehyde 3-phosphate binding By similarity
Sites
	Active site	141	1	Nucleophile By similarity
	Binding site	111	1	NAD; via amide nitrogen By similarity
	Binding site	169	1	NAD By similarity
	Binding site	171	1	Glyceraldehyde 3-phosphate By similarity
	Binding site	300	1	NAD; via carbonyl oxygen By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58838-1 [UniParc]. Last modified May 27, 2002. Version 1. Checksum: 33CDD4095B9816A2	FASTA	335	36,359
	10 20 30 40 50 60 MAKAKIAVNG YGTIGKRVAD AAQAQDDMEI IGISKTKPNY EAAVAHQLGY DIYAPAANLE 70 80 90 100 110 120 AFEKAGMPAA GSIEEMVEKA DVIVDCTPGG IGKSNKALYE KAGVKAIWQG GEDHELAGYS 130 140 150 160 170 180 FNAVANYEGA LGLDFVRVVS CNTTGLCRVI YPIDKAFGTK KVRVTLARRA TDPNDIKKGP 190 200 210 220 230 240 INAIVPDPIK LPSHHGPDVK TVIPHIDITS AAMKIPTTLM HVHTVNMELK NECTAEDVRQ 250 260 270 280 290 300 VLGSQSRVRF VGQGITSTAE IMEVARDIKR PRNDMWENCV WPDSITMHEG ELYFFQAIHQ 310 320 330 ESIVVPENVD AIRAMMELES DGAKSILKTN KAIGL

References

[1]

"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE010299 Genomic DNA. Translation: AAM06714.1.
RefSeq	NP_618234.1.
3D structure databases
HSSP	HSSP built from PDB template 1CF2 based on UniProtKB P10618.
ModBase	Search...
Genome annotation databases
GeneID	1475238.
GenomeReviews	Gene locus MA_3345 in contig AE010299_GR.
KEGG	mac:MA3345.
NMPDR	fig|188937.1.peg.3260.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P58838.
Enzyme and pathway databases
BioCyc	MACE188937:MA3345-MON.
Family and domain databases
HAMAP	MF_00559. [Tree]
InterPro	IPR000173. GlycerAld_3-P_DHase. IPR006436. Glyceraldehyde-3-P_DHase_2_arc. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF02800. Gp_dh_C. 1 hit. PF00044. Gp_dh_N. 1 hit. [Graphical view]
PIRSF	PIRSF000149. GAP_DH. 1 hit.
ProDom	PD007761. GAPDH_like. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01546. GAPDH-II_archae. 1 hit.
PROSITE	PS00071. GAPDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G3P2_METAC

Accession

Primary (citable) accession number: P58838

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	May 27, 2002
Last modified:	November 25, 2008
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)