PYC_PICPA
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 03-AUG-2022, entry version 115.
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; Saccharomycetes;
OC 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 carboxylase
RT and identification of a suppressor of the pyc phenotype.";
RL Yeast 14:647-654(1998).
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:0000250}.
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 -!- 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.
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DR EMBL; Y11106; CAA71993.1; -; Genomic_DNA.
DR AlphaFoldDB; P78992; -.
DR SMR; P78992; -.
DR PRIDE; P78992; -.
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: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; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Zinc.
FT CHAIN 1..1189
FT /note="Pyruvate carboxylase"
FT /id="PRO_0000146822"
FT DOMAIN 21..473
FT /note="Biotin carboxylation"
FT DOMAIN 143..340
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 559..826
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 1099..1174
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 315
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 567..571
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 568
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 640
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 736
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 766
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 768
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 900
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 736
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1140
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT 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
