G3P_PARBA
ID G3P_PARBA Reviewed; 338 AA.
AC Q8X1X3; C1HCH7; Q6A547;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12;
GN Name=GPD; ORFNames=PAAG_08468;
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-16; 90-107
RP AND 120-138, AND INDUCTION.
RX PubMed=15275662; DOI=10.1016/j.fgb.2004.02.002;
RA Barbosa M.S., Cunha Passos D.A., Felipe M.S.S., Jesuino R.S.A., Pereira M.,
RA de Almeida Soares C.M.;
RT "The glyceraldehyde-3-phosphate dehydrogenase homologue is differentially
RT regulated in phases of Paracoccidioides brasiliensis: molecular and
RT phylogenetic analysis.";
RL Fungal Genet. Biol. 41:667-675(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
RN [3]
RP PROTEIN SEQUENCE OF 2-16, AND INDUCTION.
RX PubMed=11418327; DOI=10.1016/s1286-4579(01)01409-5;
RA da Fonseca C.A., Jesuino R.S.A., Felipe M.S.S., Cunha D.A., Brito W.A.,
RA de Almeida Soares C.M.;
RT "Two-dimensional electrophoresis and characterization of antigens from
RT Paracoccidioides brasiliensis.";
RL Microbes Infect. 3:535-542(2001).
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:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Preferentially expressed in yeast cells, the host parasitic
CC phase. Induced during mycelium to yeast transition and negatively
CC regulated during the yeast to mycelium transition.
CC {ECO:0000269|PubMed:11418327, ECO:0000269|PubMed:15275662}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEH38741.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF396657; AAP42760.1; -; Genomic_DNA.
DR EMBL; AY061958; AAL34975.1; -; mRNA.
DR EMBL; KN294026; EEH38741.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015701183.1; XM_015846519.1.
DR AlphaFoldDB; Q8X1X3; -.
DR SMR; Q8X1X3; -.
DR STRING; 502779.Q8X1X3; -.
DR MoonProt; Q8X1X3; -.
DR PRIDE; Q8X1X3; -.
DR EnsemblFungi; EEH38741; EEH38741; PAAG_08468.
DR GeneID; 9092839; -.
DR KEGG; pbl:PAAG_08468; -.
DR eggNOG; KOG0657; Eukaryota.
DR HOGENOM; CLU_030140_0_1_1; -.
DR OrthoDB; 945145at2759; -.
DR BRENDA; 1.2.1.12; 6937.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
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; PTHR10836; PTHR10836; 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; Direct protein sequencing; Glycolysis; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed; partial"
FT /evidence="ECO:0000269|PubMed:11418327"
FT CHAIN 2..338
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145565"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 36470 MW; 51822C121240B2F6 CRC64;
MVVKVGINGF GRIGRIVFRN AVEHDDVEIV AVNDPFIETK YAAYMLKYDS THGQFKGDIQ
HSSSNNLTVN NKTIHFYQER DPANIPWGKH GVDYVVESTG VFTTTEKAKA HLSGGAKKVI
ISAPSADAPM FVMGVNEKSY RPDISVLSNA SCTTNCLAPL AKVIHDNFGI AEGLMTTIHS
YTATQKTVDG PSHKDWRGGR TAAQNIIPSS TGAAKAVGKV IPALNGKLTG MAMRVPTANV
SVVDLTCRTE KPVTYDQIKA AVKAASEGEL KGILGYSEDA LVSTDLNGDP RSSIFDASAG
IALNDRFVKL ISWYDNEWGY SRRVLDLIAY IAKVDAGK
