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Database: UniProt
Entry: A0A124IU53_9CREN
LinkDB: A0A124IU53_9CREN
Original site: A0A124IU53_9CREN 
ID   A0A124IU53_9CREN        Unreviewed;       262 AA.
AC   A0A124IU53;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU003388};
DE            EC=1.2.1.59 {ECO:0000256|RuleBase:RU003388};
DE   Flags: Fragment;
GN   ORFNames=AT708_04065 {ECO:0000313|EMBL:KUO90036.1};
OS   Pyrobaculum sp. OCT_11.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=1714259 {ECO:0000313|EMBL:KUO90036.1, ECO:0000313|Proteomes:UP000054659};
RN   [1] {ECO:0000313|EMBL:KUO90036.1, ECO:0000313|Proteomes:UP000054659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA   Inskeep W.P.;
RT   "The distribution, diversity and function of predominant Thermoproteales in
RT   high-temperature environments of Yellowstone National Park.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|RuleBase:RU003388};
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         Evidence={ECO:0000256|RuleBase:RU003388};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869,
CC       ECO:0000256|RuleBase:RU003388}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|RuleBase:RU003388}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003388}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU003388}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUO90036.1}.
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DR   EMBL; LOBY01000101; KUO90036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124IU53; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000054659; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:RHEA.
DR   GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
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   HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01546; GAPDH-II_archae; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU003388};
KW   Glycolysis {ECO:0000256|RuleBase:RU003388};
KW   NAD {ECO:0000256|RuleBase:RU003388}; NADP {ECO:0000256|RuleBase:RU003388};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003388}.
FT   DOMAIN          70..215
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02800"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KUO90036.1"
SQ   SEQUENCE   262 AA;  29153 MW;  7A6B3953445D3329 CRC64;
     DATPEDVGRE NKERHYQRFD KPVIFQGGEE ADVAEVSFNA LANYEEARGR RYVRVVSCNT
     TGITRVLSAL LLNGMGVKKA RIFIARRGAD PKEHKKGPIN DVVPNPATVP SHHGPDVQTI
     LRDIDIVTMA VAVPVTIMHM HMAYLELDST YTRDAVLEAF AKTPRIYLAD VGAGFQSLAQ
     IIEYARDLGR PRADFPEVAL FRDSVTVRGN ELYLMYGVHQ ESIVVPENVD AIRAIFGTLP
     KWTSIEKTDK TLKLSTNGKV YA
//
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