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Database: UniProt
Entry: A0A1E7YEB0_9MYCO
LinkDB: A0A1E7YEB0_9MYCO
Original site: A0A1E7YEB0_9MYCO 
ID   A0A1E7YEB0_9MYCO        Unreviewed;      1131 AA.
AC   A0A1E7YEB0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   05-DEC-2018, entry version 13.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=BA059_07875 {ECO:0000313|EMBL:OFB40929.1};
OS   Mycolicibacterium sp. (ex Dasyatis americana).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1866905 {ECO:0000313|EMBL:OFB40929.1, ECO:0000313|Proteomes:UP000176008};
RN   [1] {ECO:0000313|EMBL:OFB40929.1, ECO:0000313|Proteomes:UP000176008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dasyatis americana {ECO:0000313|EMBL:OFB40929.1,
RC   ECO:0000313|Proteomes:UP000176008};
RA   Innis C., Stuber T., Robbe-Austerman S.;
RT   "Mycobacterium fortuitum complex isolated from captive Southern
RT   Stingray (Dasyatis americana).";
RL   Submitted (JUN-2016) 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
CC       and 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(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         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|PIRNR:PIRNR001594};
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OFB40929.1}.
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DR   EMBL; MAIH01000070; OFB40929.1; -; Genomic_DNA.
DR   RefSeq; WP_070185881.1; NZ_MAIH01000070.1.
DR   EnsemblBacteria; OFB40929; OFB40929; BA059_07875.
DR   Proteomes; UP000176008; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
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   Gene3D; 3.20.20.70; -; 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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 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|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000176008};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:OFB40929.1}.
FT   DOMAIN        1    449       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      121    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      524    793       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1056   1130       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   COILED      171    194       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    292    292       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       533    533       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       703    703       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       732    732       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       734    734       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     117    117       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     200    200       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     235    235       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     605    605       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     870    870       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1131 AA;  121064 MW;  8AD216ED2357A838 CRC64;
     MVDKVLVANR GEIAIRAFRA AYELGLSTVA VYPYEDRNSQ HRLKADESYQ IGEEGHPVRA
     YLSVEEIIRV AREAGADAIY PGYGFLSENP DLARACEHAG ITFVGPSADV LELTGNKARA
     IAAARTAGLP VLASSAPSSS VSELLAAAES MSFPVFVKAV AGGGGRGMRR VNDLTDLKEA
     IEAASREAES AFGDPTVFLE QAVINPRHIE VQILADTQGN VIHLFERDCS VQRRHQKVIE
     LAPAPDLDPD LRERICADAV AFARQIGYSC AGTVEFLLDE RGRHVFIECN PRIQVEHTVT
     EEITDVDLVS SQLRIAGGQS LSDLGLAQGA LKIRGAALQC RITTEDPSNG FRPDTGRITA
     YRSPGGAGVR LDGGTNLGAE VAAHFDSMLV KLTCRGRDFS TAVARARRAV AEFRIRGVST
     NIPFLAAVLE DPDFVAGRVT TSFIEERPQL LTARGSADRG TRILNYLADV TVNQPHGPRP
     SVVYPRDKLP ECDLSIAPPP GSKQRLTELG PEGFATWLRN SRAISVTDTT FRDAHQSLLA
     TRVRTSGLLR VAPYIARTMP QLLSVECWGG ATYDVSLRFL KQDPWERLAA LREALPNICL
     QMLLRGRNTV GYTPYPEAVT HAFVDEAAAT GVDIFRIFDA LNNVDSMRPA IDAVRHTGTT
     IAEVAMSYTG DLSDPGESLY TLDYYLRLAE QIVEAGAHVL AVKDMAGLLR APAAATLVSA
     LKSRFDLPVH VHTHDTPGGQ LATYVAAWMA GADAVDGAAA PLAGTTSQPA LSSIVAAAAH
     TEYDTGLSLH AVCDLEPYWE ALRKVYAPFD VAASVPPSPT GRVYAHEIPG GQLSNLRQQA
     IALGLGDRFE DIEANYAAAD RMLGRLVKVT PSSKVVGDLA LAMVGAGIDA DDFAANPARH
     DIPDSVIGFL RGELGDPAGG WPEPLRTKAL DGRGPSRPIQ ELSAEDEAVL TAPGPKRQAT
     LNRLLFPGPT AEFEAHRDEF GDTSRLSANQ FFYGLRHGEE HRVKLEPGVE LLIGLEAISE
     PDERGMRTVM CILNGQLRPI VVADRSIASE VPVAEKADRA DPAHIGAPFA GVVTVNVAEG
     DTVEAGQSVA TIEAMKMEAA ITAPESGTVT RIAVARTAQV EGGDLLVVVG Q
//
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