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Entry: A0A1S6IPT5_9LACT
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Original site: A0A1S6IPT5_9LACT 
ID   A0A1S6IPT5_9LACT        Unreviewed;      1143 AA.
AC   A0A1S6IPT5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=cfiB {ECO:0000313|EMBL:AQS53568.1};
GN   ORFNames=BW727_101201 {ECO:0000313|EMBL:AQS53568.1};
OS   Jeotgalibaca dankookensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Jeotgalibaca.
OX   NCBI_TaxID=708126 {ECO:0000313|EMBL:AQS53568.1, ECO:0000313|Proteomes:UP000188993};
RN   [1] {ECO:0000313|EMBL:AQS53568.1, ECO:0000313|Proteomes:UP000188993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EX-07 {ECO:0000313|EMBL:AQS53568.1,
RC   ECO:0000313|Proteomes:UP000188993};
RX   PubMed=24554638; DOI=10.1099/ijs.0.057059-0;
RA   Lee D.G., Trujillo M.E., Kang H., Ahn T.Y.;
RT   "Jeotgalibaca dankookensis gen. nov., sp. nov., a member of the family
RT   Carnobacteriaceae, isolated from seujeot (Korean traditional food).";
RL   Int. J. Syst. Evol. Microbiol. 64:1729-1735(2014).
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; CP019728; AQS53568.1; -; Genomic_DNA.
DR   RefSeq; WP_062472250.1; NZ_CP019728.1.
DR   AlphaFoldDB; A0A1S6IPT5; -.
DR   STRING; 708126.BW727_101201; -.
DR   KEGG; jda:BW727_101201; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000188993; Chromosome.
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:InterPro.
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; PS00866; CPSASE_1; 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|PIRNR:PIRNR001594};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001594};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188993}.
FT   DOMAIN          1..451
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..316
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          529..797
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1072..1141
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         538
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         610
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         707
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         736
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         738
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         871
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         707
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1107
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1143 AA;  127241 MW;  A7005E1CEE5E7E3B CRC64;
     MKKVLVANRG EIAIRIFRAL AELGIGTVGI YAQEDEGSVH RFKADEAYLV GSGKKPIEAY
     LDIEGIIALS KEAQVDAIHP GYGFLSENIH FARRCQEEGI KFIGPDLHHL DIFGDKIKAK
     QAAIAAGIQS IPGSDGPVSN AEEVLDFAVQ YGYPIIIKAA LGGGGRGMRV AHNDEEAKDG
     FIRARSEALS AFGDDHIYVE KYIQNPKHIE VQILGDEHGN IVHLYERDCS VQRRHQKVVE
     VAPCINMADD LRQEICQAAL QLMQHVGYVN AGTVEFLVAD DQYYFIEVNP RVQVEHTITE
     MITGIDIVQA QIKIAQGQDL HKDIHIPEQA NIPLIGAAIQ CRITTEDPLN NFFPDTGKIN
     TYRSPGGFGI RLDAGNGFQG TVVSPFFDSL LVKACVQAPT FSDAVRKMER ALTEFRIRGV
     KTNIPFLRNV IQNPIFASGE ATTTFIDETP SLFVFPETLN RGNKMLAYLG NTTVNGFPGI
     SHAPKKFYEK PRLPKKIILP EKELVTAKTI LDQEGPEAVS QWVKQQSKVL LTDTTFRDAH
     QSLLATRVRT TDLLAIAKQT QEGMPQLFSN EMWGGASFDV AYRFLSEDPW DRLRKLRKLM
     PHTLFQMLFR GSNAVGYQNY PDNVLKAFIT QAAEAGIDVF RLFDSLNWTA QIEKSIQYVR
     DVNKIAEAAI CYTGDVNDPN QSKYTIAYYK DMARELEHMG AHIIAIKDMA GLLKPQAAYR
     LISELKETVS LPIHLHTHDT SGNGIYTLTE AIRAGVDIVD VAQSALSGTT SQPSMSSLYY
     ALEGSSLAPD LTIENVQEIN RYWEDVRTYY DGFETGIQTT STEVYRHQMP GGQYTNLQQQ
     AKSVGLEDSW DTVKEMYASV NQLFGDIVKV TPSSKVVGDM ALFMVQNHLT EADIYERGED
     LSFPQSVVSF FKGDLGQPTG GFPKELQAII LKDQKPLTVR PGSLRQPTDF KKVSMELAEI
     IGRQPSEEDV LSYLMYPDVF LGYCDTFKKF GDVTKLDTPT FFHGMRKGEQ IEVVIEKGKT
     LIIKLNQIGE PDAEGMRILY FELNGQGREI EIKDASITST KAIRKKAEPT NKEHIGSTMP
     GSVLEILVVK GDRVKKGDPV IITEAMKMET TIRSTINGVI DQIYVTANDR IEAGDLLIEI
     KPK
//
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