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Database: UniProt
Entry: W5XRL3_9CORY
LinkDB: W5XRL3_9CORY
Original site: W5XRL3_9CORY 
ID   W5XRL3_9CORY            Unreviewed;      1143 AA.
AC   W5XRL3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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   ORFNames=CCASEI_03495 {ECO:0000313|EMBL:AHI19279.1};
OS   Corynebacterium casei LMG S-19264.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1285583 {ECO:0000313|EMBL:AHI19279.1, ECO:0000313|Proteomes:UP000019226};
RN   [1] {ECO:0000313|EMBL:AHI19279.1, ECO:0000313|Proteomes:UP000019226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG S-19264 {ECO:0000313|EMBL:AHI19279.1,
RC   ECO:0000313|Proteomes:UP000019226};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium casei LMG S-19264 (=DSM
RT   44701).";
RL   Submitted (FEB-2013) 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 + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00024172};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC         Evidence={ECO:0000256|ARBA:ARBA00024172};
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};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   EMBL; CP004350; AHI19279.1; -; Genomic_DNA.
DR   RefSeq; WP_025387143.1; NZ_CP004350.1.
DR   AlphaFoldDB; W5XRL3; -.
DR   STRING; 1285583.CCASEI_03495; -.
DR   GeneID; 82876883; -.
DR   KEGG; ccg:CCASEI_03495; -.
DR   PATRIC; fig|1285583.3.peg.679; -.
DR   eggNOG; COG1038; Bacteria.
DR   HOGENOM; CLU_000395_0_1_11; -.
DR   OrthoDB; 9760256at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000019226; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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   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; 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   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; PS00188; BIOTIN; 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   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:0000313|EMBL:AHI19279.1}.
FT   DOMAIN          8..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          128..324
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          532..801
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1066..1143
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         541
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         613
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         711
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         740
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         742
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         875
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         711
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1109
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1143 AA;  124739 MW;  A445AB266D1AC710 CRC64;
     MVDSALPSFK KILVANRGEI AVRAFRAAYE TGAKTVAIYP REDRNSFHRA FADEAVRIGV
     EGQPVKAYLN IDEVIRAAKK SGADAVYPGY GFLSERAELA RACEAEGIKF IGPSPSTLDL
     TGDKAAAVEA ATAAGLPTLH DSKASTDVDE LFEASKDFEY PMFAKALAGG GGRGMRFIEN
     EKEFKERVAE ASREAETAFG DGRVYLETAV IKPQHIEVQI LADGKGNVMH LFERDCSVQR
     RHQKVVEIAP APYLDPELRD RICQDAVNFC KHINYEGAGT VEFLVDERGN HVFIEMNPRV
     QVEHTVTEEV TGIDIVKSQM QIAAGATLED LGLSQEEVRL NGFALQCRIT TEDPNNGFRP
     DTGTLTAYRS PGGAGVRLDG ATSVGAEISP NFDSLLVKMT CRGKDFPQAV QRSRRALKEF
     NIAGVATNIG FLRALLREPD FVSKRIDTGF INNHPDLLKA PPASNEQDRI LEYLADVTVN
     QPNGKRPTDL RPFDKLPKID RQNVNLPRGS RDDLLELGPQ GFAEKLRNQS ALAVTDTTFR
     DAHQSLLATR VRGTALVTAA EHVARLTPEL YSVEAWGGAT YDVAMRFLFE DPWQRLDLLR
     EAMPNVNIQM LLRGRNTVGY TPYPDSVCRA FVQEAAKSGV DVFRIFDALN DVSQMRPAIE
     AVLETNTTVA EVAMAYSGNL SDPNEKLYTL DYYLNLAEEI VKTGAHVLAI KDMAGLLRPE
     SAATLVTELR KNFDLPIHVH THDTAGGQLA TYYAAAMAGA DAVDGASAPL AGTTSQPSLS
     AIVGAFANTS RDTKIDLEAI SNMEPYWEAV RQLYAPFENG IPGPTGRVYK HEIPGGQLSN
     LRAQASALGL ADRFEVIEDN YAAVNEMLGR PTKVTPSSKV VGDLALHLVG AGVDPADFEE
     NPTRYDIPDS VIAFLRGELG TPPGGWPPLR DKILSGRTGE LKLSEVPAEE AAHLESEDSS
     ERRPSLNRLL FPKQWDEFNE FRRHYGNTEA LNDADFFYGL NEGEERIIHL FPEGSNDRAD
     LKQMVVRLDA VGEPDEKGMR SVILNVNGQI RPLKVRDQSV ESVTATVEKA DPKQEGHVAA
     PFSGVVNPTV QAGDEVKAGD QVAVIEAMKM EASISATKDG KIERVAIAQA TKVEGGDLIA
     VIS
//
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