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
//