ID A0A1A6HCE9_NEOLE Unreviewed; 303 AA.
AC A0A1A6HCE9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000256|ARBA:ARBA00031890};
GN ORFNames=A6R68_17302 {ECO:0000313|EMBL:OBS76248.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS76248.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS76248.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS76248.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS76248.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) 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=1.2.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-
CC cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089,
CC Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:149494; Evidence={ECO:0000256|ARBA:ARBA00024287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685;
CC Evidence={ECO:0000256|ARBA:ARBA00024287};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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:OBS76248.1}.
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DR EMBL; LZPO01034950; OBS76248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A6HCE9; -.
DR STRING; 56216.A0A1A6HCE9; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF111; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 2.
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 Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 2..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 33
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 SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 303 AA; 32649 MW; 2528443E7A3D7DBE CRC64;
MVKVGVNGFG QIGRLVTRAA FQSGKVEIVA INDPFIDPNY MVYMFQYDST HGKFNSTVKA
ENGKLIINRK AITIFQEQDP ANIKWDEAGA KYVVGCTGVF TTMEKTGAHL KGGAKRVIIS
PPSADTPTFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTAHAIT
ATQKAVDGPS GKLWREGRGA AQNIIPASTS AAKAVGKVIP ELNGNLMGMA FHVPIPSVSV
VDLTCRNLLS MMISRRCDPP PPKKTFDAGA GTALNDNSAK FISWYDNEFS YSNRVVDLMA
SKE
//
