ID E3LPS0_CAERE Unreviewed; 1175 AA.
AC E3LPS0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN Name=Cre-pyc-1 {ECO:0000313|EMBL:EFP05831.1};
GN ORFNames=CRE_27332 {ECO:0000313|EMBL:EFP05831.1}, FL81_14719
GN {ECO:0000313|EMBL:POM34457.1}, FL82_11341
GN {ECO:0000313|EMBL:OZF78780.1}, GCK72_018113
GN {ECO:0000313|EMBL:KAF1751559.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|EMBL:EFP05831.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|EMBL:EFP05831.1};
RG The Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:POM34457.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM34457.1};
RX PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Reproductive Mode and the Evolution of Genome Size and Structure in
RT Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005323-e1005323(2015).
RN [4] {ECO:0000313|EMBL:POM34457.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX356 {ECO:0000313|EMBL:POM34457.1};
RX PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA Ahearne T.E., Cutter A.D., Phillips P.C.;
RT "Correction: Reproductive Mode and the Evolution of Genome Size and
RT Structure in Caenorhabditis Nematodes.";
RL PLoS Genet. 11:e1005497-e1005497(2015).
RN [5] {ECO:0000313|EMBL:OZF78780.1, ECO:0000313|Proteomes:UP000216624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX439 {ECO:0000313|EMBL:OZF78780.1,
RC ECO:0000313|Proteomes:UP000216624};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:POM34457.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PX356 {ECO:0000313|EMBL:POM34457.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:KAF1751559.1, ECO:0000313|Proteomes:UP000483820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX506 {ECO:0000313|EMBL:KAF1751559.1,
RC ECO:0000313|Proteomes:UP000483820};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KAF1751559.1};
RA Teterina A.A., Willis J.H., Phillips P.C.;
RT "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC carboxylation of the covalently attached biotin in the first step and
CC the transfer of the carboxyl group to pyruvate in the second.
CC {ECO:0000256|PIRNR:PIRNR001594}.
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:0000256|PIRNR:PIRNR001594};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953,
CC ECO:0000256|PIRNR:PIRNR001594};
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DR EMBL; DS268412; EFP05831.1; -; Genomic_DNA.
DR EMBL; WUAV01000005; KAF1751559.1; -; Genomic_DNA.
DR EMBL; NMWX01000510; OZF78780.1; -; Genomic_DNA.
DR EMBL; LFJK02001048; POM34457.1; -; Genomic_DNA.
DR RefSeq; XP_003114493.1; XM_003114445.1.
DR AlphaFoldDB; E3LPS0; -.
DR STRING; 31234.E3LPS0; -.
DR EnsemblMetazoa; CRE27332.1; CRE27332.1; WBGene00052363.
DR GeneID; 9818999; -.
DR KEGG; crq:GCK72_018113; -.
DR CTD; 9818999; -.
DR eggNOG; KOG0369; Eukaryota.
DR HOGENOM; CLU_000395_0_1_1; -.
DR OMA; YAIQSRV; -.
DR OrthoDB; 1129179at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR Proteomes; UP000216624; Unassembled WGS sequence.
DR Proteomes; UP000483820; Chromosome v.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 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 NCBIfam; TIGR01235; pyruv_carbox; 1.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
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; SSF51569; Aldolase; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000256|ARBA:ARBA00023317};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 31..481
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 151..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 559..828
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1099..1174
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 323
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 568
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 640
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 737
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 767
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 769
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 904
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 737
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1140
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1175 AA; 129127 MW; 1BED7535501C7DAB CRC64;
MRFARIPPIF ANVVRQTQHR TYANGVVKPR EFNKVMVANR GEIAIRVFRA LTELNKTSVA
IYAEQDKNSI HRLKADESYL VGKGLPPVAA YLTIDQIIET ALKHDIDAIH PGYGFLSERS
DFAAACQNAG IVFIGPSPDV MARMGDKVAA RQAAIEAGVQ VVPGTPGPIT TADEAIEFAK
QYGTPIILKA AYGGGGRGIR RVDKLEEVEE AFRRSYSEAQ AAFGDGSLFV EKFVERPRHI
EVQLLGDHHG NIVHLYERDC SVQRRHQKVV EIAPAPALPE GVREKILADA LRLARHVGYQ
NAGTVEFLVD QKGNYYFIEV NARLQVEHTV TEEITGVDLV QAQIRIAEGK SLEDLKLSQD
TIHTTGSAIQ CRVTTEDPAK GFQPDSGRIE VFRSGEGMGI RLDSASAFAG SVISPHYDSL
MVKVIASARN HPNAAAKMIR ALKEFRIRGV KTNIPFLLNV LRQPSFLDAS VDTYFIDEHP
ELFQFKPSQN RAQKLLSYLG EVKVNGPTTP LATDLKPAHV SPPIPYIPAG AKPPAGLRNV
LVQKGPAEFA KEVRKTPGCM ITDTTFRDAH QSLLATRVRT YDMAAISPFV AQSFTNLFSL
ENWGGATFDV SMRFLHECPW ERLRTLRELI PNIPFQCLLR GANAMGYSNY PDNVIYKFCD
LAVKNGMDVF RVFDSLNYLP NLLVGMEAVG KAGGVVEAAI AYTGDVTDKS RDKYDLKYYL
NLADQLVKAQ AHILSIKDMA GVLKPEAAKL LIGALRDKFP DIPIHVHTHD TSGAGVAAML
ECAKAGADVV DAAVDSMSGM TSQPSMGAIV ASLQGTKHDT GLSLDDISKY SAYWESARQF
YAPFESATTM KSGNADVYKH EIPGGQYTNL QFQAFSLGLG PQFDDVKRMY REANLVLGDI
IKVTPSSKIV GDLAQFMVQN GLTRETLVDR ADDLSFPKSV VDFMQGNVGQ PPYGFPEPLR
TKVLRGKPKV DGRPGENAKP VDLDAVKVEL EEKHGRPLSE EDVMSYSMFP SVFDEFETFR
QQYGPVDKLP TRLFLTGLDI AEEVDVEIES GKTLAIQLLA EGKLNKRGER EVFFDLNGQM
RSIFVVDKEA SKEIVTRPRA LPGVRGHIGA PMPGDVLELK IKEGDKVTKK QPLFVLSAMK
MEMVIDSPIA GTVKKVHAGQ GTKCTAGDLV IEIEP
//