G3P2_METAC
ID G3P2_METAC Reviewed; 335 AA.
AC P58838;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE Short=GAPDH 2;
DE EC=1.2.1.59;
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase 2;
GN Name=gapB; OrderedLocusNames=MA_3345;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE010299; AAM06714.1; -; Genomic_DNA.
DR RefSeq; WP_011023275.1; NC_003552.1.
DR AlphaFoldDB; P58838; -.
DR SMR; P58838; -.
DR STRING; 188937.MA_3345; -.
DR EnsemblBacteria; AAM06714; AAM06714; MA_3345.
DR GeneID; 1475238; -.
DR KEGG; mac:MA_3345; -.
DR HOGENOM; CLU_069533_0_0_2; -.
DR InParanoid; P58838; -.
DR OMA; NAIVPNP; -.
DR OrthoDB; 32079at2157; -.
DR PhylomeDB; P58838; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR InterPro; IPR000846; DapB_N.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01113; DapB_N; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..335
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145719"
FT ACT_SITE 141
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 140..142
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 195..196
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 36359 MW; 33CDD4095B9816A2 CRC64;
MAKAKIAVNG YGTIGKRVAD AAQAQDDMEI IGISKTKPNY EAAVAHQLGY DIYAPAANLE
AFEKAGMPAA GSIEEMVEKA DVIVDCTPGG IGKSNKALYE KAGVKAIWQG GEDHELAGYS
FNAVANYEGA LGLDFVRVVS CNTTGLCRVI YPIDKAFGTK KVRVTLARRA TDPNDIKKGP
INAIVPDPIK LPSHHGPDVK TVIPHIDITS AAMKIPTTLM HVHTVNMELK NECTAEDVRQ
VLGSQSRVRF VGQGITSTAE IMEVARDIKR PRNDMWENCV WPDSITMHEG ELYFFQAIHQ
ESIVVPENVD AIRAMMELES DGAKSILKTN KAIGL
