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Database: UniProt
Entry: D3DZM8_METRM
LinkDB: D3DZM8_METRM
Original site: D3DZM8_METRM 
ID   D3DZM8_METRM            Unreviewed;       338 AA.
AC   D3DZM8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
DE            Short=GAPDH {ECO:0000256|HAMAP-Rule:MF_00559};
DE            EC=1.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559};
GN   Name=gap {ECO:0000256|HAMAP-Rule:MF_00559,
GN   ECO:0000313|EMBL:ADC47706.1};
GN   OrderedLocusNames=mru_1856 {ECO:0000313|EMBL:ADC47706.1};
OS   Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM
OS   13430 / OCM 146 / M1) (Methanobacterium ruminantium).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC47706.1, ECO:0000313|Proteomes:UP000008680};
RN   [1] {ECO:0000313|EMBL:ADC47706.1, ECO:0000313|Proteomes:UP000008680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1
RC   {ECO:0000313|Proteomes:UP000008680};
RX   PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA   Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA   Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA   Janssen P.H., Dey D., Attwood G.T.;
RT   "The genome sequence of the rumen methanogen Methanobrevibacter
RT   ruminantium reveals new possibilities for controlling ruminant methane
RT   emissions.";
RL   PLoS ONE 5:E8926-E8926(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADH;
CC         Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
CC         ECO:0000256|SAAS:SAAS01127777};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10296, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00559, ECO:0000256|SAAS:SAAS01127759};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
CC       ECO:0000256|SAAS:SAAS01167718}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176915}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176910}.
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DR   EMBL; CP001719; ADC47706.1; -; Genomic_DNA.
DR   RefSeq; WP_012956654.1; NC_013790.1.
DR   STRING; 634498.mru_1856; -.
DR   EnsemblBacteria; ADC47706; ADC47706; mru_1856.
DR   GeneID; 8771526; -.
DR   KEGG; mru:mru_1856; -.
DR   PATRIC; fig|634498.28.peg.1856; -.
DR   eggNOG; arCOG00493; Archaea.
DR   eggNOG; COG0057; LUCA.
DR   HOGENOM; HOG000223361; -.
DR   KO; K00150; -.
DR   OMA; NAIVPNP; -.
DR   OrthoDB; 32079at2157; -.
DR   BioCyc; MRUM634498:G1GFU-1884-MONOMER; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000008680; 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:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
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   Complete proteome {ECO:0000313|Proteomes:UP000008680};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176917};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01167717};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
KW   ECO:0000256|SAAS:SAAS01176916};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
KW   ECO:0000256|SAAS:SAAS01167721};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176912,
KW   ECO:0000313|EMBL:ADC47706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008680}.
FT   DOMAIN        2    141       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   NP_BIND      11     12       NAD. {ECO:0000256|HAMAP-Rule:MF_00559,
FT                                ECO:0000256|PIRSR:PIRSR000149-3}.
FT   REGION      140    142       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   REGION      195    196       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   ACT_SITE    141    141       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00559, ECO:0000256|PIRSR:PIRSR000149-
FT                                1}.
FT   BINDING     111    111       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     169    169       NAD. {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     302    302       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
SQ   SEQUENCE   338 AA;  37035 MW;  1A598726B77E0BC8 CRC64;
     MKSVAINGFG TIGKRVADAV AAQDDMKVIG VSKTRPNFEA RTAVEEKGYP LYIGIPEREP
     LFKEAGIEIA GTVEDMIQEA DIVVDCTPGN IGPQNLEMYK KAGVKAIYQG GEDHELTGLS
     FNSFANYDDS YGADYARVVS CNTTGLTRTL HTLNPLVDIK KVRAVMVRRG SDPSEIKKGP
     INAIVPNPPK VPSHHGPDVQ TVMKGIDVTT MALLVPTTLM HQHNLMVEIG NDVTKEEVIE
     ALEKRSRVMV VEAAAGLDST AALMEYAKDL GRSRNDLYEI PVWKESINVV DNELFYMQAV
     HQESDVVPEN VDAIRAMLEM ESDNEKSIAK TNKAMGIF
//
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