ID I2JW62_DEKBR Unreviewed; 1185 AA.
AC I2JW62;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=AWRI1499_2889 {ECO:0000313|EMBL:EIF47214.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF47214.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF47214.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF47214.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(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};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIF47214.1}.
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DR EMBL; AHIQ01000165; EIF47214.1; -; Genomic_DNA.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000004997; 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-UniPathway.
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; 1.10.10.2790; -; 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 Gene3D; 1.10.472.90; Conserved carboxylase domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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}; Pyruvate {ECO:0000313|EMBL:EIF47214.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004997}.
FT DOMAIN 22..474
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 144..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 565..832
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1103..1178
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 316
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 574
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 646
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 742
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 772
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 774
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 906
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 742
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1144
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1185 AA; 129515 MW; 50301F29970E3DC6 CRC64;
MSNSEFPSLQ KLRNQSQILP GQYNKILVAN RGEIPIRIFR SAHELGMHTV AVYSYEDRLS
MHRFKADEAY QIGKKGQYSP VQAYLAMDEI IDIAKKHGVS MIHPGYGFLS ENEEFAAKVE
NAGLIWVGPS PEVIESLGDK VSARVLAAKC XVPTVPGTPG PIEDVEEAKX FVKKYGYPVI
IKAAYGGGGR GMRVVHEGDD IVDAFHRASS EAKSAFGNGT CFLERFLIHP KHIEVQLLAD
SYGNTVHLFE RDCSVQRRHQ KVIEMAPSKT LPDDVRNSIL ADAVKLAKTA HFRSAGTAEF
LVDTKGRHYF IEVNPRIQVE HTITEEITGI DIVSAQIQIA AGASLTDMGL LQDKITTRGF
AIQCRITTED PAKNFQPDTG KIEVYRSAGG NGIRLDGGNG FVGSVISPHY DSLLVKCTAH
ASNFEVTRRK MVRALIEFRI RGVKTNIPFL IAVLTHPVFQ QGSCWTTFID DTPSLFDMIS
SKNRAQKLLG YIAEMCVNGS SVKGQVGVPR LHEEAXIPAI TDPATGASID VASLPPPARS
SGWRDVIVSS GPEEFAXRVR RNNGVLIMDT TWRDAHQSLL ATRVRTIDLL NIAPSTAYAF
TNAFALECWG GATFDVSMRF LHEDPWQRLR KMRAAVPNIP FQMLLRGANG VGYASLPDNA
IDHFVKQAKD NGVDIFRVFD ALNDLEQLKV GVDAVKKAGG VVEATVCYSG DMLQPGKKYN
LDYYMQTVGQ IVKMGTHVLG IKDMAGTMKP AAARLLIGSI RKAYPDLPIH LHTHDSAGTG
VSTYVAAAEA GVDVVDCAVN SMSGLTSQPS MSAFIAAVDG RFATGIPESA ARELDXYWAE
MRLLYSCFGA DLKGPDPEIY KTEIPGGQLT NLIFQAQQVG LGDQWAATKA AYTEANRLLG
DIVKVTPTSK VVGDLAQFMV SNHLSGPDVE RLASELDFPD SVLDFFQGLM GTPYGGFPEP
LRTNVLRGKR RKLTCRPGLE LKPFDLQQVR NDLHARFGPE IDECDVASYN MYPKVYEDWR
SVLEKYGDLS VLPTRFFLAA PKIGEEINVN IEEGKTLIIK LIAVGDLNQE TGTRDVYFQM
NGEMRKVAVQ DKKAGVEKVT KPKADGHNPN EVGSPMSGVI VEVKANVGDD VAKGDPLCVL
SAMKMEMVVS APTAGRVLDI FIKKDENVEG GDLLVKLGHP GTPDA
//
