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Database: UniProt
Entry: P78992
LinkDB: P78992
Original site: P78992 
ID   PYC_PICPA               Reviewed;        1189 AA.
AC   P78992;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   05-DEC-2018, entry version 108.
DE   RecName: Full=Pyruvate carboxylase;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
GN   Name=PYC1;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9639311;
RX   DOI=10.1002/(SICI)1097-0061(199805)14:7<647::AID-YEA269>3.0.CO;2-L;
RA   Menendez J., Delgado J., Gancedo C.;
RT   "Isolation of the Pichia pastoris PYC1 gene encoding pyruvate
RT   carboxylase and identification of a suppressor of the pyc phenotype.";
RL   Yeast 14:647-654(1998).
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
DR   EMBL; Y11106; CAA71993.1; -; Genomic_DNA.
DR   ProteinModelPortal; P78992; -.
DR   SMR; P78992; -.
DR   PRIDE; P78992; -.
DR   eggNOG; ENOG410IU5D; Eukaryota.
DR   eggNOG; COG1038; LUCA.
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   1189       Pyruvate carboxylase.
FT                                /FTId=PRO_0000146822.
FT   DOMAIN       21    473       Biotin carboxylation.
FT   DOMAIN      143    340       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      559    826       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1099   1174       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      567    571       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    315    315       {ECO:0000250}.
FT   METAL       568    568       Divalent metal cation. {ECO:0000250}.
FT   METAL       736    736       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       766    766       Divalent metal cation. {ECO:0000250}.
FT   METAL       768    768       Divalent metal cation. {ECO:0000250}.
FT   BINDING     139    139       ATP. {ECO:0000250}.
FT   BINDING     223    223       ATP. {ECO:0000250}.
FT   BINDING     258    258       ATP. {ECO:0000250}.
FT   BINDING     640    640       Substrate. {ECO:0000250}.
FT   BINDING     900    900       Substrate. {ECO:0000250}.
FT   MOD_RES     736    736       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1140   1140       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   1189 AA;  131400 MW;  8B6E858079657914 CRC64;
     MAEEDYLPVY QLRRDSSLLG TMNKILVANR GEIPIRIFRT AHELSMNTVA IYSHEDRLSM
     HRLKADEAYV IGERGQYSPV QAYLAIDEII KIAVKHNVNM IHPGYGFCSE NSEFARKVEE
     NGILWVGPSD TVIDAVGDKV SARNLAYAAN VPTVPGTPGP IEDVAQATAF VEEYGYPVII
     KAAFGGGGRG MRVVREGDDI EDAFLRASSE AKTAFGNGTV FIERFLDKPK HIEVQLLADN
     YGNVIHLFER DCSVQRRHQK VARNCSAKTL PVEVRNAILN DAVKLAKTAN YRNAGTAEFL
     VDSQNRHYFI EINPRIQVEH TITEEITGVD IVAAQIQIAA GASLEQLGLL QEKITTRGFA
     IQCRITTEDP TKNFQPDTGK IEVYRSSGGN GVRLDGGNGF AGAVISPHYD SMLVKCSTSG
     SNYEIRRRKM IRALVEFRIR GVKTNIPFLL ALLTHPVFMT SECWTTFIDD TPELFKILTS
     QNRAQKLLAY LGDLAVNGSS IKGQIGLPKL HKEADIPSIT DINGDVIDVS IPPPDGWRQF
     LLEKGPEQFA QQVRAFPGLM IMDTTWRDAH QSLLATRVRT HDLLNIAPAT SYALHHAFAL
     ECWGGATFDV SMRFLHEDPW QRLRKLRKAV PNIPFSMLLR GGNGVAYYSL PDNAIDHFLK
     QAKDTGVDVF RVFDALNDIE QLKVGVDAVK KAGGVVEATM CYSGDMLKPG KKYNLEYYIN
     LATEIVEMGT HILAVKDMAG TLKPTAAKQL ISALRRKFPS LPIHVHTHDS AGTGVASMVA
     CARAGADVVT VRVNSMSGMT SQPSMSAFIA SLDGEIETGI PEANAREIDA YWAEMRLLYS
     CFEADLKGPD PEVYQHEIPG GQLTNLLFQA QQVGLGEKWV ETKKAYEAAN RLLGDIVKVT
     PTSKVVGDLA QFMVSNKLSS EDVERLASEL DFPDSVLDFF EGLMGTPYGG FPEPLRTNVI
     SGKRRKLTSR PGLTLEPYNI PAIREDLEAR FSKVTENDVA SYNMYPKVYE AYKKQQELYG
     DLSVLPTRNF LSPPKIDEER HVTIVTIETR KTLIIKCMAE GELSQSSGTR EVYFELNGEM
     RKVTVEDKNG AVETITRPKA DAHNPNEIGA PMAGVVVEVR VHENGEVKKG DPIAVLSAMK
     MEMVISSPVA GRIGQIAVKE NDSVDASDLI PKSSRLSKLL MFIILIILY
//
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