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Database: UniProt
Entry: A0A059MRG3_9NOCA
LinkDB: A0A059MRG3_9NOCA
Original site: A0A059MRG3_9NOCA 
ID   A0A059MRG3_9NOCA        Unreviewed;       339 AA.
AC   A0A059MRG3; A0A0F6VIV6; N1M5N0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00021022, ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   Name=gap {ECO:0000313|EMBL:UYF91989.1};
GN   ORFNames=OCS65_15820 {ECO:0000313|EMBL:UYF91989.1};
OS   Rhodococcus aetherivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=191292 {ECO:0000313|EMBL:UYF91989.1, ECO:0000313|Proteomes:UP001163947};
RN   [1] {ECO:0000313|EMBL:UYF91989.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N1 {ECO:0000313|EMBL:UYF91989.1};
RA   Jiang W.;
RT   "The genome sequence of Rhodococcus aetherivorans N1.";
RL   Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC       phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC       NAD. The first reaction step involves the formation of a hemiacetal
CC       intermediate between G3P and a cysteine residue, and this hemiacetal
CC       intermediate is then oxidized to a thioester, with concomitant
CC       reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC       second NAD, and the thioester is attacked by a nucleophilic inorganic
CC       phosphate to produce BPG. {ECO:0000256|ARBA:ARBA00003501}.
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   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
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; CP106982; UYF91989.1; -; Genomic_DNA.
DR   RefSeq; WP_006937692.1; NZ_CP130480.1.
DR   GeneID; 83621915; -.
DR   Proteomes; UP001163947; Chromosome.
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:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43148; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160}.
SQ   SEQUENCE   339 AA;  35855 MW;  152189E3FA914D5C CRC64;
     MTVRVGVNGF GRIGRNFFRA VEAQRALGTT DIEIVAVNDL TDNATLAHLL KYDSILGRLP
     QDVSLDGEDT IVVGDHRIKA LEVKEGPAAL PWGDLGVDVV VESTGIFTDA SKAKGHLDAG
     AKKVIISAPA KGEDLTVVMG VNDDKYDGSQ NIISNASCTT NCLGPIAKVL DDSFGIVKGL
     MTTVHAYTQD QNLQDGPHKD LRRARAAALN VVPTGTGAAK AIGLVLPQLV GKLDGYALRV
     PIPTGSVTDL TANLATPASI EEINAAMKAA AEGPLKGILK YTEDEIVSSD IVTDPHSSIY
     DAGLTKVIDD QVKIVSWYDN EWGYSNRLVD LIGLVSKSL
//
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