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Database: UniProt
Entry: A0A086YMB7_9FIRM
LinkDB: A0A086YMB7_9FIRM
Original site: A0A086YMB7_9FIRM 
ID   A0A086YMB7_9FIRM        Unreviewed;      1229 AA.
AC   A0A086YMB7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   03-MAY-2023, entry version 32.
DE   RecName: Full=pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN   ORFNames=DK28_0205015 {ECO:0000313|EMBL:KFD41770.1};
OS   Peptococcaceae bacterium SCADC1_2_3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1487582 {ECO:0000313|EMBL:KFD41770.1, ECO:0000313|Proteomes:UP000027084};
RN   [1] {ECO:0000313|EMBL:KFD41770.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41770.1};
RA   Tan B.F., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KFD41770.1, ECO:0000313|Proteomes:UP000027084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCADC1_2_3 {ECO:0000313|EMBL:KFD41770.1};
RA   Tan B., Charchuk R., Li C., Nesbo C., Abu-Laban N., Foght J.;
RT   "Draft genome sequence of an unculturable Firmicutes affiliated with
RT   Peptococcaceae sorted using a microfluidic device from methanogenic alkane-
RT   degrading cultures.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFD41770.1}.
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DR   EMBL; JJNX02000019; KFD41770.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086YMB7; -.
DR   STRING; 1487582.HY00_05225; -.
DR   Proteomes; UP000027084; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   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   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   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   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; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KFD41770.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027084}.
FT   DOMAIN          10..453
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          126..324
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          539..814
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   1229 AA;  138303 MW;  7BC18240E5662CDC CRC64;
     MRRVKPPTIQ GIKIGVANRG IPALRVGRAI REMGGIYVAF YTEQDKTAPH VTKSDEAYNL
     QSESGYLNID EIIWIAKQHN VKALHPGWGF AAEDSRFPSL CRENGIIFIG PSEAPMKKLG
     NKIRAREIAQ SVSVPIIPGS QGTVALREAK QVAQEIGYPV MLKSEGGGGG KGIVLINSSE
     EVEYHFEKAS IIAEASFGNP NLYIEKFLSS VRHLEIQAVC DSFGNAVVLD ERDCSAQRKN
     QKILEITPSP WKKMNEGLRR ALKEATLRIV SAVGYDSIVT FEFLVDEELN YYFIEANTRL
     QVEHGISELL YNIDLVEEMI RIAFGEKLRL KEEELKPRGF AMQCRINFED PQNDFQPSAG
     EITRYLSPGG EGIRVDSCVF GGYEFPKAYD SLGCLLMAYG RTWGKTLSIM ERALSEYIAG
     GLKTTIPFHK RIISHPKFRA GEADTKFIDN EPELMVYRET VPEELRLSRL MVEITAKGYN
     PYLGLGVYRK FGDSKLGPVY FDVSSLVKNV AGDRSYRPLF YPGEHRDKVL KLLRNSKYVE
     FCNTTPRDVT QSESGNRFRL FSDRLIGPML DRCGYFSIEN GGGAHYHVAM LGCMTDPWEE
     AAEWNSFAPY TQKQILVRST NLLGYAPQTK EVMKRTAEMI IKHYHVIRCF DFLNHVQNMV
     PLAEIVLQAE NRIFEPAISL SWAQGFDVPH YLSVLEDILF MVGRIIKCEK SEASKKIILG
     LKDMAGVCPP SFIKSLISAM LDKYPELVIQ YHRHATDGLA VPALGAAAQA GAKILDVADG
     PSVRFYSQAA VMPVVAYVEG ELGLKTRLDK EKIRETAFVL KQIMPIYDRY CRPIFLGVDH
     DVTLHGLPGG ATASSQEEAL KQGYTFLLPS ILQVLELYRK IIRYHDVTPG SQITWTNSYL
     MVVKAYERGG LPEVQRITGL LKKVALTPEE ELDHQTKVDR KIIFSHANDA LKNLLLGKFG
     KLPLGWPPEW VYQSVFSNDW QDAITQRTEE SPLNFLPPVE IDEIEMELTR HIGRKPTENE
     LINYLNHPGE VLKLIKNLEL YGNPNMLPDD IWFEGLEPGI PREFRASDGK VHNIEVMNIG
     DISKDGIRRV QYRLDYEVFV EEVPVAASVK EGKKGVEMAD KDNPYHIAAP FNADLWIVYK
     KAGDSVQAGE KVLSLTLMKI EYGVASAVDG AVKRVLVFAD YKSDKKMVPV LQGQLLIELA
     PPYECCPRCK AELNKEDKFC SKCGREINR
//
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