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Database: UniProt
Entry: E3LPS0_CAERE
LinkDB: E3LPS0_CAERE
Original site: E3LPS0_CAERE 
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
//
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