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Database: UniProt
Entry: J4I919_9APHY
LinkDB: J4I919_9APHY
Original site: J4I919_9APHY 
ID   J4I919_9APHY            Unreviewed;      1197 AA.
AC   J4I919;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=FIBRA_02421 {ECO:0000313|EMBL:CCM00391.1};
OS   Fibroporia radiculosa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fibroporiaceae; Fibroporia.
OX   NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00391.1, ECO:0000313|Proteomes:UP000006352};
RN   [1] {ECO:0000313|EMBL:CCM00391.1, ECO:0000313|Proteomes:UP000006352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00391.1,
RC   ECO:0000313|Proteomes:UP000006352};
RX   PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA   Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA   Diehl S.V.;
RT   "Short-read sequencing for genomic analysis of the brown rot fungus
RT   Fibroporia radiculosa.";
RL   Appl. Environ. Microbiol. 78:2272-2281(2012).
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   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC       the ATP-dependent carboxylation of the covalently attached biotin in
CC       the first step and the transfer of the carboxyl group to pyruvate in
CC       the second. {ECO:0000256|ARBA:ARBA00002380}.
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|ARBA:ARBA00000564,
CC         ECO:0000256|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953,
CC         ECO:0000256|PIRNR:PIRNR001594};
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DR   EMBL; HE796980; CCM00391.1; -; Genomic_DNA.
DR   RefSeq; XP_012179674.1; XM_012324284.1.
DR   AlphaFoldDB; J4I919; -.
DR   STRING; 599839.J4I919; -.
DR   GeneID; 24095302; -.
DR   HOGENOM; CLU_000395_1_0_1; -.
DR   InParanoid; J4I919; -.
DR   OrthoDB; 1129179at2759; -.
DR   Proteomes; UP000006352; 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:UniProtKB-KW.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 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; IPR000089; Biotin_lipoyl.
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   InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; 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   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006352}.
FT   DOMAIN          47..503
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          173..370
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          582..856
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        345
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         591
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         663
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         765
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         795
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         797
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         930
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         765
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1166
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1197 AA;  130523 MW;  95B833E06FCE40A2 CRC64;
     MPADTGATAT LHPPRLAAMF AGSPSAPGTP VHSIQTMRRK AAGHSGPLTK ILVANRGEIA
     IRVFRTSHEL AMHTVAIYSF EDRLSAHRQK ARTLCSADEA YQVGKGLTPV AAYLAQDDII
     RIALEHGVDM IHPGYGFLSE NAEFARKVEM AGIAFVGPSP EVIDQLGDKT KARTVALKVG
     VPVVPGTPGP VDSYVEADSF IKEYGFPVII KAAMGGGGRG MRVVREQSDF AASFERAVSE
     AKSAFGDGTV FIERFLERPR HIEVQLLADG EGNTIHLFER DCSVQRRHQK VVEVAPATHL
     PEEVRQAILA DAIKLAKSVG YRNAGTAEFL VDQMGRHYFI EINPRIQVEH TITEEITGID
     IVAAQIQIAA GATLPQLGLS QEAITKRGFA IQCRVTTEDA ATGFQPDTGK IEVYRSAGGN
     GVRLDASSGF AGAQITPHYD SLLVKVSVSG TTYEVARRKM LRALVEFRIR GVKTNIPFLF
     RLLTHDFIDD TPELFKLVQS QNRAQKLLAY LGDLAVNGSS IKGQQGEPGL KDDIVVPVFQ
     NRDDPEGPPL DASLPCEKGW RNIIVEQGPE AFARAVREYP GVLIMDTTWR DAHQSLLATR
     LRTIDIANIA KETSYALSNA FSLECWGGAT FDVAMRFLYE DPWERLRALR KLVPNIPLQA
     LVRGANGVGY TSYPDNAIYD FSKKAVENGL DIFRVFDSLN YIENVSGTLL KLGIDAAKKA
     GGVVEAAVCY SGDVANPKLT KYTLQYYLDF VDQLVAEGIH ILSIKDMAGL LKPEAAKILI
     GAIREKYPDL PIHVHSHDTA GISTASMLAA AAAGADVIDV AIDSMSGLTS QPPMGAICSA
     LEQTGMGTGI RYADIQALNV YWSQVRMLYG CFEANVRASD SSVFDHEMPG GQYTNLMFQA
     AQLGLGTQWT EVKKKYIEAN DMCGNVIKVT PTSKVVGDFA QWMVSNGFSK QDVLDRAEQL
     DFPSSVVEFF QGYLGQPVGG FPEPLRTKII RDKPRIDGRP GTNMVPVDFK KTKAELRSKF
     GKHITDADVT SYVMYPKVFE EYQNFVEKYG DLSVIPTRYF LGRPDIGEEM HISIEKGKTL
     IIRLMAVGPV VEGRAQRDVW FEVNGEVRAV SVEDKNSAVE TVSREKATSD PGSVGAPMSG
     VVVEVRVKEG SEIKKGDPVC VMSAMKACSP VSGHIKRVVV HEGDSINQGD LVVEIVH
//
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