GenomeNet

Database: UniProt
Entry: Q8X1T3
LinkDB: Q8X1T3
Original site: Q8X1T3 
ID   PYC_PICAN               Reviewed;        1175 AA.
AC   Q8X1T3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 90.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
GN   Name=PYC;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=12589070; DOI=10.1091/mbc.E02-07-0417;
RA   Ozimek P., Van Dijk R., Latchev K., Gancedo C., Wang D.Y.,
RA   Van Der Klei I.J., Veenhuis M.;
RT   "Pyruvate carboxylase is an essential protein in the assembly of yeast
RT   peroxisomal oligomeric alcohol oxidase.";
RL   Mol. Biol. Cell 14:786-797(2003).
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction,
CC       involving the ATP-dependent carboxylation of the covalently
CC       attached biotin in the first step and the transfer of the carboxyl
CC       group to pyruvate in the second. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
DR   EMBL; AF221670; AAL69566.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8X1T3; -.
DR   SMR; Q8X1T3; -.
DR   MoonProt; Q8X1T3; -.
DR   PRIDE; Q8X1T3; -.
DR   PhylomeDB; Q8X1T3; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
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   Gene3D; 3.20.20.70; -; 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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 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   3: Inferred from homology;
KW   ATP-binding; Biotin; Cytoplasm; Gluconeogenesis; Ligase;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding; Zinc.
FT   CHAIN         1   1175       Pyruvate carboxylase.
FT                                /FTId=PRO_0000146821.
FT   DOMAIN       22    474       Biotin carboxylation.
FT   DOMAIN      144    341       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      561    828       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1099   1174       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      569    573       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    316    316       {ECO:0000250}.
FT   METAL       570    570       Divalent metal cation. {ECO:0000250}.
FT   METAL       738    738       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       768    768       Divalent metal cation. {ECO:0000250}.
FT   METAL       770    770       Divalent metal cation. {ECO:0000250}.
FT   BINDING     140    140       ATP. {ECO:0000250}.
FT   BINDING     224    224       ATP. {ECO:0000250}.
FT   BINDING     259    259       ATP. {ECO:0000250}.
FT   BINDING     642    642       Substrate. {ECO:0000250}.
FT   BINDING     902    902       Substrate. {ECO:0000250}.
FT   MOD_RES     738    738       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1140   1140       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   1175 AA;  129811 MW;  AEC5FDF96F408989 CRC64;
     MAQVEDYSSL HRLRKNSEIL SNANKILVAN RGEIPIRIFR SAHELSMQTV AIYSHEDRLS
     MHRLKADEAY VIGARGQYSP VQAYLQIDEI INIALEHNVS MIHPGYGFLS ENSEFARKVE
     DSGMIWIGPP HNVIDAVGDK VSARNLAGKC NVPVVPGTDG PIDSVEQAQE FVDKYGYPVI
     IKAAFGGGGR GMRVVREGES IADAFQRATS EAKTAFGNGT CFIERFLDKP KHIEVQLLAD
     NYGNVIHLFE RDCSVQRRHQ KVVEIAPAKT LPVEVRDAIL TDAVKLAKAA NYRNAGTAEF
     LVDNQNRHYF IEINPRIQVE HTITEEVTGV DIVAAQIQIA AGASLQQLGL LQDKITTRGF
     AIQCRITTED PAKNFQPDTG KIEVYRSSGG NGVRLDGGNG FAGAIISPHY DSMLVKCSTS
     GSNYEIARRK MIRALVEFRI RGVKTNIPFL LALLTHPTFV SGDCWTTFID DTPSLFEMVQ
     SKNRAQKLLS YLADLCVNGS SIKGQIGLPK LTRDADIPVI HDINGWDIDI KNTPPPESFR
     QYLLDYGPEQ FANQIRAFDG CLIMDTTWRD AHQSLLATRV RTIDLLNIAP ATAHAFRYAF
     ALECWGGATF DVAMRFLHED PWDRLRKLRK AVPNIPFQML LRGANGVAYS SLPDNAIDHF
     VKQAKDAGVD IFRVFDALND LEQLKVGVDA VKKAGGVVEA TVCYSGDMLK PGKKYNLKYY
     LETVDKIMEM GTHLLGIKDM AGTLKPAAAK LLISSIRKKY PSVPIHVHTH DSAGTGVITY
     VACALAGADV VDCAVNSMSG LTSQPSMSAF IAALDNEINT GITEQNAREI DAYWSEMRLL
     YSCFEADLKG PDPEVYNHEI PGGQLTNLLF QAQQVGLGEK WLETKKAYEE ANMLLGDIVK
     VTPTSKVVGD LAQFMVSNKL SPKDVERLAS ELDFPDSVLD FFEGLMGTPY GGFPEPLRTN
     ILAGKRRKLT RRPGLELEPF DLKKIKEELQ SRFGNSITEC DVASYNMYPK VFESFKKIQE
     KYGDLSVLPT RFFLAPPKLN EEISVEIEQG KTFVIKVMAI GDLSPQTGTR EVYFEFNGEM
     RKVTVEDKLA AVETVTRPKA DAHNPNEVGA PMAGVVIEVR VHPGVEVKKG DPLCVLSAMK
     MEMVISSPVS GRVGEVIVHE NDSVDAGDLI CKITK
//
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