G3P_MYCTU
ID G3P_MYCTU Reviewed; 339 AA.
AC P9WN83; L0T894; O06822; P64178;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:24161676};
DE Short=GAPDH {ECO:0000303|PubMed:24161676};
DE EC=1.2.1.12 {ECO:0000269|PubMed:24161676};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:24161676};
GN Name=gap; OrderedLocusNames=Rv1436; ORFNames=MTCY493.18c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP CYS-158; CYS-162 AND HIS-185, AND REACTION MECHANISM.
RX PubMed=24161676; DOI=10.1016/j.abb.2013.10.007;
RA Wolfson-Stofko B., Hadi T., Blanchard J.S.;
RT "Kinetic and mechanistic characterization of the glyceraldehyde 3-phosphate
RT dehydrogenase from Mycobacterium tuberculosis.";
RL Arch. Biochem. Biophys. 540:53-61(2013).
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:0000269|PubMed:24161676}.
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:0000269|PubMed:24161676};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for Na(2)PO(4) {ECO:0000269|PubMed:24161676};
CC KM=6.2 mM for Na(2)AsO(4) {ECO:0000269|PubMed:24161676};
CC Note=kcat is 1670 min(-1) for dehydrogenase activity with G3P.
CC {ECO:0000269|PubMed:24161676};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P54226}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44195.1; -; Genomic_DNA.
DR PIR; G70915; G70915.
DR RefSeq; NP_215952.1; NC_000962.3.
DR RefSeq; WP_003407390.1; NZ_NVQJ01000038.1.
DR AlphaFoldDB; P9WN83; -.
DR SMR; P9WN83; -.
DR STRING; 83332.Rv1436; -.
DR PaxDb; P9WN83; -.
DR DNASU; 886632; -.
DR GeneID; 45425414; -.
DR GeneID; 886632; -.
DR KEGG; mtu:Rv1436; -.
DR TubercuList; Rv1436; -.
DR eggNOG; COG0136; Bacteria.
DR OMA; NCVAPMA; -.
DR PhylomeDB; P9WN83; -.
DR BRENDA; 1.2.1.12; 3445.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR43148; PTHR43148; 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..339
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145671"
FT ACT_SITE 158
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:24161676"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 157..159
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 188
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 203
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 216..217
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 239
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 320
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 185
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000305|PubMed:24161676"
FT MUTAGEN 158
FT /note="C->A: Loss of dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:24161676"
FT MUTAGEN 162
FT /note="C->A: Same dehydrogenase activity compared to the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:24161676"
FT MUTAGEN 185
FT /note="H->A: Loss of dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:24161676"
SQ SEQUENCE 339 AA; 35956 MW; 362D0D59E90A4588 CRC64;
MTVRVGINGF GRIGRNFYRA LLAQQEQGTA DVEVVAANDI TDNSTLAHLL KFDSILGRLP
CDVGLEGDDT IVVGRAKIKA LAVREGPAAL PWGDLGVDVV VESTGLFTNA AKAKGHLDAG
AKKVIISAPA TDEDITIVLG VNDDKYDGSQ NIISNASCTT NCLAPLAKVL DDEFGIVKGL
MTTIHAYTQD QNLQDGPHKD LRRARAAALN IVPTSTGAAK AIGLVMPQLK GKLDGYALRV
PIPTGSVTDL TVDLSTRASV DEINAAFKAA AEGRLKGILK YYDAPIVSSD IVTDPHSSIF
DSGLTKVIDD QAKVVSWYDN EWGYSNRLVD LVTLVGKSL
