ID C6H4X5_AJECH Unreviewed; 1128 AA.
AC C6H4X5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 13-SEP-2023, entry version 66.
DE RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN ORFNames=HCDG_00296 {ECO:0000313|EMBL:EER44717.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER44717.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second.
CC {ECO:0000256|PIRNR:PIRNR001594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|PIRNR:PIRNR001594};
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DR EMBL; GG692419; EER44717.1; -; Genomic_DNA.
DR AlphaFoldDB; C6H4X5; -.
DR STRING; 544712.C6H4X5; -.
DR VEuPathDB; FungiDB:HCDG_00296; -.
DR eggNOG; KOG0369; Eukaryota.
DR HOGENOM; CLU_000395_0_1_1; -.
DR OMA; YAIQSRV; -.
DR Proteomes; UP000002624; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR NCBIfam; TIGR01235; pyruv_carbox; 1.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:EER44717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002624}.
FT DOMAIN 45..497
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 167..364
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 583..851
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 339
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 592
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 664
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 760
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 790
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 792
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 925
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
SQ SEQUENCE 1128 AA; 123986 MW; 9949BFEB1C5FA721 CRC64;
MTSFFSGFPP GQHESAVDDL AEDHSRHPAH HSVHGRLRAN STIMQFNKIL VANRGEIPIR
IFRTAHELSL QTVAVYSYED RLSMHRQKAD EAYIIGKRGQ YTPVGAYLAG DEIIKIAVQH
GVHLIHPGYG FLSENAEFAR NVEKAGLVFV GPTPDTIDTL GDKVSARRLA IKCGVPVVPG
TPGPVERFEE VKAFTDQYGF PIIIKAAFGG GGRGMRVVRE QETLQDAFER ATSEAKSAFG
NGTVFVERFL DKPKHIEVQL LGDNHGNIVH LYERDCSVQR RHQKVVEVAP AKDLPVDVRD
TILADAVKLA KSVNYRNAGT AEFLVDQQNR YYFIEINPRI QVEHTITEEI TGIDIVAAQI
QIAAGASLEQ LGLTQDRIST RGFAIQCRIT TEDPTKGFSP DTGKIEVYRS AGGNGVRLDG
GNGFAGAIIT PHYDSMLVKC TCRGFTYEIV RRKMLRALIE FRIRGVKTNI PFLASVLTHP
TFIEGTCWTT FIDDSPELFS MIGSQNRAQK LLAYLGDIAV NGSSIKGQIG EPKFKGDINM
PTIVDESNEP VDVTVPCSQG WKKIVDEQGP AAFAKAVRAN KGCLIMDTTW RDAHQSLLAT
RVRTVDLLNI AKETSYAYSN AYSLECWGGA TFDVAMRFLY EDPWDRLRKM RKAVPNIPFQ
MLLRGANGVA YSSLPDNAIY HFCKQAKRYG VDIFRVFDAL NDIDQLEVGM KAVAAAGGVI
EATICYSGDM LNPSKKYNLD YYLTLVDKIV KIGTHVLGIK DMAGVLKPQA ATLLVGAIRQ
RYPDLPIHVH THDSAGTGVA SMVACAQAGA DAVDAATDSM SGMTSQPSVG AIIASLEGTD
LDPKLNIRNI RAIDSYWAQL RLLYSPFEAG LTGPDPEVYE HEIPGGQLTN LIFQAHQLGL
GAQWAETKKA YEQANDLLGD IVKVTPTSKV VGDLAQFMVS NKLTPDDVIA RAGELDFPGS
VLEFFEGLMG QPYGGFPEPL RSRALRERRK LNDRPGLHLE PLDLAKIKND LREKFGTATE
CDVASYAMYP KVFEDYRKFV AKYGDLSVLP TKYFLARPQI GEEILRRTGA GQGAYLKLPG
RWGAAIRADP GQRRGVFMKM NRRGSGQVSV DDKPCCGSTD ASRPKGGI
//
