ID E4NTU1_HALBP Unreviewed; 358 AA.
AC E4NTU1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Hbor_26990 {ECO:0000313|EMBL:ADQ68246.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ68246.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|EMBL:ADQ68246.1, ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
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|ARBA:ARBA00001820, ECO:0000256|HAMAP-
CC Rule:MF_00559, 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|ARBA:ARBA00001295, ECO:0000256|HAMAP-
CC Rule:MF_00559, 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|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
CC ECO:0000256|RuleBase:RU003388}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|HAMAP-Rule:MF_00559,
CC ECO:0000256|RuleBase:RU003388}.
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DR EMBL; CP001690; ADQ68246.1; -; Genomic_DNA.
DR AlphaFoldDB; E4NTU1; -.
DR STRING; 469382.Hbor_26990; -.
DR KEGG; hbo:Hbor_26990; -.
DR eggNOG; arCOG00493; Archaea.
DR HOGENOM; CLU_069533_0_0_2; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000006663; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1.
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 NCBIfam; TIGR01546; GAPDH-II_archae; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR SMART; SM00846; Gp_dh_N; 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|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_00559,
KW ECO:0000256|RuleBase:RU003388};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00559};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00559}; Reference proteome {ECO:0000313|Proteomes:UP000006663}.
FT DOMAIN 1..137
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 336..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 8..9
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 136..138
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 191..192
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 298
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
SQ SEQUENCE 358 AA; 38367 MW; 3B52EE600B33CCCA CRC64;
MGVNGYGTIG KRVADAVDAQ PDMEVIGVAK TQPNFEAHTA VKRGYPMYAA IPERMPLFSE
AGIDVEGAVD EMVADADIVV DCTPSGIGAE NKALYESHDT PAIFQGGEDA DVGEVSFNAR
ANYDDARGVD YVRTVSCNTT GLSRIIAPLR EEYGVEKVRA TLVRRGGDPG QNSRGPINDI
LPNPISIPSH HGPDVNTIFP DLAIDTLGLK VPATLMHVHS LNVTLEDDVT AAHVRQLLES
ESRVYVIPEG LGIDGAGKLK DFALDAGRPR GDLWENCVWG ESIAVEGRDL YLFQAIHQES
DVIPENVDAI RAMTESVDQA ESMVTTDDYL GVGITGDPSG FSNEDEAEAV TETEIADD
//
