ID M4MCW4_CAMJU Unreviewed; 332 AA.
AC M4MCW4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN Name=gapA {ECO:0000313|EMBL:AGG58987.1};
GN ORFNames=Cj1403c {ECO:0000313|EMBL:AGG58987.1};
OS Campylobacter jejuni subsp. jejuni.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=32022 {ECO:0000313|EMBL:AGG58987.1};
RN [1] {ECO:0000313|EMBL:AGG58987.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H704 {ECO:0000313|EMBL:AGG58985.1}, H73020
RC {ECO:0000313|EMBL:AGG58986.1}, P179a {ECO:0000313|EMBL:AGG58987.1},
RC P569a {ECO:0000313|EMBL:AGG58988.1}, and P694a
RC {ECO:0000313|EMBL:AGG58989.1};
RA Mohan V., Stevenson M.;
RT "Campylobacter jejuni genomes exhibit notable GC variation within
RT housekeeping genes.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; KC405089; AGG58985.1; -; Genomic_DNA.
DR EMBL; KC405114; AGG58986.1; -; Genomic_DNA.
DR EMBL; KC405139; AGG58987.1; -; Genomic_DNA.
DR EMBL; KC405164; AGG58988.1; -; Genomic_DNA.
DR EMBL; KC405189; AGG58989.1; -; Genomic_DNA.
DR RefSeq; WP_002780453.1; NZ_SZUS01000007.1.
DR SMR; M4MCW4; -.
DR KEGG; cjw:PJ18_07170; -.
DR KEGG; cjy:QZ67_01538; -.
DR PATRIC; fig|32022.144.peg.1540; -.
DR OMA; YGYTCNM; -.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
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 NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 3..150
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 208..209
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 231
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 332 AA; 36302 MW; D5FFC5A6FAF4B3BD CRC64;
MAVKVAINGF GRIGRCVARI ILERNDIELV AINDTTDIEL TKYLFKYDTV HGEFKGSVDS
EGDDLVVNGK KIKVFKSRNV KDLDFAKHGA QIVLECTGAH LTMAKCQEFI DMGVQKVIMS
APAKDDTPTY VLGVNSELYK GESIISNASC TTNCLGPVCR VLQDNFGIEK GLMTTIHAYT
NGQSIIDAKA KDKRRSRAAA QNIIPTSTGA AKAMKLVMPE LNGKLHGQSM RVPVIDVSSV
DLTAQLSRKV SKDEINEAFR KAAATNLKGI LMVDDDERVS SDFITCSYGA IVASDLTQVI
ADDFIKVIAW YDNEWGYSSR LVDMAVYIAN KA
//
