PYC_PICAN
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 03-AUG-2022, entry version 96.
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; Saccharomycetes;
OC 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, 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; 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}.
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DR EMBL; AF221670; AAL69566.1; -; Genomic_DNA.
DR AlphaFoldDB; 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: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..1175
FT /note="Pyruvate carboxylase"
FT /id="PRO_0000146821"
FT DOMAIN 22..474
FT /note="Biotin carboxylation"
FT DOMAIN 144..341
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 561..828
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 316
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 569..573
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 642
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 738
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
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 770
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 902
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 738
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 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
