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Database: UniProt
Entry: Q18KG2_HALWD
LinkDB: Q18KG2_HALWD
Original site: Q18KG2_HALWD 
ID   Q18KG2_HALWD            Unreviewed;       357 AA.
AC   Q18KG2;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 109.
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=gap1 {ECO:0000313|EMBL:CAJ51488.1};
GN   Synonyms=gap {ECO:0000256|HAMAP-Rule:MF_00559};
GN   OrderedLocusNames=HQ_1360A {ECO:0000313|EMBL:CAJ51488.1};
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ51488.1, ECO:0000313|Proteomes:UP000001975};
RN   [1] {ECO:0000313|EMBL:CAJ51488.1, ECO:0000313|Proteomes:UP000001975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA   Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ51488.1; -; Genomic_DNA.
DR   RefSeq; WP_011570644.1; NC_008212.1.
DR   STRING; 362976.HQ_1360A; -.
DR   EnsemblBacteria; CAJ51488; CAJ51488; HQ_1360A.
DR   GeneID; 4194009; -.
DR   KEGG; hwa:HQ_1360A; -.
DR   eggNOG; arCOG00493; Archaea.
DR   eggNOG; COG0057; LUCA.
DR   HOGENOM; HOG000223361; -.
DR   KO; K00150; -.
DR   OMA; NAIVPNP; -.
DR   BioCyc; HWAL362976:G1G1J-378-MONOMER; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000001975; 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:UP000001975};
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:CAJ51488.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001975}.
FT   DOMAIN        2    140       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      139    141       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   REGION      194    195       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   ACT_SITE    140    140       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00559, ECO:0000256|PIRSR:PIRSR000149-
FT                                1}.
FT   BINDING     110    110       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     168    168       NAD. {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     301    301       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
SQ   SEQUENCE   357 AA;  37824 MW;  93F94BC53BD4AAC9 CRC64;
     MIRVGVNGYG TIGKRVADAV ALQPDMEVVG VAKTKPNFEA HTADQRGYEM YAAIPDRAPL
     FGDAGVELAG AVDELVAAAD IMIDCTPSGI GAENKSLYES YDTPAIFQGG EDATIAEVSF
     NARANYAAAC GTDSVRVVSC NTTGLSRVIA PLQEAYGIEQ VRTTLVRRGG DPSQNSRGPI
     NDILPNPISI PSHHGPDVNT IFPDLAIDTL GLKVPATLMH VHALNVTLKS DVTVAHVRQL
     LEEESRIYVI SEGMGIDGAG KLKDFAHDAG RPRGDIWENC VWGESIAISG RDLYFFQAIH
     QESDVIPENI DAIRAMTESA TAAESIELTN RTLGVGITGS PVGVVDTDHS GVEAADD
//
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