PYC1_CAEEL
ID PYC1_CAEEL Reviewed; 1175 AA.
AC O17732;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Pyruvate carboxylase 1;
DE EC=6.4.1.1;
DE AltName: Full=Pyruvic carboxylase 1;
DE Short=PCB 1;
GN Name=pyc-1 {ECO:0000312|EMBL:AAF60326.1}; ORFNames=D2023.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:AAF60326.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11761713; DOI=10.3109/10425170109047568;
RA Liao V.H.-C., Freedman J.H.;
RT "Characterization of a cadmium-inducible isoform of pyruvate carboxylase
RT from Caenorhabditis elegans.";
RL DNA Seq. 12:137-145(2001).
RN [2] {ECO:0000312|EMBL:CAB02872.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP PROTEIN SEQUENCE OF 286-292; 452-462; 495-503; 718-728; 750-756; 892-902;
RP 1021-1032 AND 1053-1063, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [4]
RP INTERACTION WITH SIR-2.2 AND SIR-2.3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
RA Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
RA Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
RT "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals
RT interact with pyruvate carboxylase and other acetylated biotin-dependent
RT carboxylases.";
RL Mitochondrion 13:705-720(2013).
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|UniProtKB:P11154}.
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:0000305};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000250|UniProtKB:P11154};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P11154};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Interacts with sir-2.2 and sir-2.3.
CC {ECO:0000269|PubMed:23438705}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11154}.
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DR EMBL; AF237467; AAF60326.1; -; mRNA.
DR EMBL; Z81052; CAB02872.1; -; Genomic_DNA.
DR PIR; T20346; T20346.
DR RefSeq; NP_001256376.1; NM_001269447.1.
DR AlphaFoldDB; O17732; -.
DR SMR; O17732; -.
DR BioGRID; 44641; 15.
DR DIP; DIP-25614N; -.
DR IntAct; O17732; 3.
DR STRING; 6239.D2023.2a.1; -.
DR iPTMnet; O17732; -.
DR EPD; O17732; -.
DR PaxDb; O17732; -.
DR PeptideAtlas; O17732; -.
DR PRIDE; O17732; -.
DR EnsemblMetazoa; D2023.2a.1; D2023.2a.1; WBGene00004258.
DR EnsemblMetazoa; D2023.2a.2; D2023.2a.2; WBGene00004258.
DR UCSC; D2023.2.1; c. elegans.
DR WormBase; D2023.2a; CE09072; WBGene00004258; pyc-1.
DR eggNOG; KOG0369; Eukaryota.
DR GeneTree; ENSGT00900000141164; -.
DR HOGENOM; CLU_000395_0_1_1; -.
DR InParanoid; O17732; -.
DR OMA; YAIQSRV; -.
DR OrthoDB; 254436at2759; -.
DR PhylomeDB; O17732; -.
DR BRENDA; 6.4.1.1; 1045.
DR Reactome; R-CEL-196780; Biotin transport and metabolism.
DR Reactome; R-CEL-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR PRO; PR:O17732; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004258; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; O17732; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
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; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
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; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Biotin; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW Ligase; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Pyruvate; Reference proteome; Zinc.
FT CHAIN 1..1175
FT /note="Pyruvate carboxylase 1"
FT /id="PRO_0000239937"
FT DOMAIN 31..481
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255"
FT DOMAIN 151..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 559..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 323
FT /evidence="ECO:0000255"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
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 737
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 767
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 769
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 904
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 737
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; 129285 MW; DE3D21194C21E6AF CRC64;
MRFSRIPPIF ANVVRQTHYR NYANGVIKPR EFNKVMVANR GEIAIRVFRA LTELNKTSVA
IYAEQDKNSM HRLKADEAYL VGKGLPPVAA YLTIDQIIET ALKHNIDAIH PGYGFLSERS
DFAAACQNAG IVFIGPSPDV MARMGDKVAA RQAAIEAGVQ VVPGTPGPIT TADEAVEFAK
QYGTPIILKA AYGGGGRGIR RVDKLEEVEE AFRRSYSEAQ AAFGDGSLFV EKFVERPRHI
EVQLLGDHHG NIVHLYERDC SVQRRHQKVV EIAPAPALPE GVREKILADA LRLARHVGYQ
NAGTVEFLVD QKGNYYFIEV NARLQVEHTV TEEITGVDLV QAQIRIAEGK SLDDLKLSQE
TIQTTGSAIQ CRVTTEDPAK GFQPDSGRIE VFRSGEGMGI RLDSASAFAG SVISPHYDSL
MVKVIASARN HPNAAAKMIR ALKKFRIRGV KTNIPFLLNV LRQPSFLDAS VDTYFIDEHP
ELFQFKPSQN RAQKLLNYLG EVKVNGPTTP LATDLKPAVV SPPIPYIPAG AKPPTGLRDV
LVQRGPTEFA KEVRSRPGCM ITDTTFRDAH QSLLATRVRT YDMAAISPFV AQSFNGLFSL
ENWGGATFDV SMRFLHECPW ERLQTLRKLI PNIPFQCLLR GANAMGYSNY PDNVIYKFCE
LAVKNGMDVF RVFDSLNYLP NLLVGMEAVG KAGGVVEAAI AYTGDVTDKS RDKYDLKYYL
NLADQLVKAQ AHILSIKDMA GVLKPEAAKL LIGALRDKFP DIPIHVHTHD TSGAGVAAML
ECAKAGADVV DAAVDSMSGM TSQPSMGAIV ASLQGTKHDT GLSLDDISKY SAYWESTRQL
YAPFECATTM KSGNADVYKH EIPGGQYTNL QFQAFSLGLG PQFDEVKRMY REANLVLGDI
IKVTPSSKIV GDLAQFMVQN NLTRETLVDR ADDLSFPKSV VDFMQGNVGQ PPYGFPEPLR
TKVLRGKPKV DGRPGENAKP VDLDAVKVEL EEKHGRTLSE EDVMSYSMFP TVFDEFETFR
QQYGPVDKLP TRLFLTGLEI AEEVDVEIES GKTLAIQLLA EGKLNKRGER EVFFDLNGQM
RSIFVVDKEA SKEIVTRPRA LPGVRGHIGA PMPGDVLELK IKEGDKVTKK QPLFVLSAMK
MEMVIDSPIA GTVKAIHAPQ GTKCSAGDLV VEVEP
