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
//