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Database: UniProt
Entry: A0A0P1E699_9RHOB
LinkDB: A0A0P1E699_9RHOB
Original site: A0A0P1E699_9RHOB 
ID   A0A0P1E699_9RHOB        Unreviewed;      1145 AA.
AC   A0A0P1E699;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-JUN-2019, entry version 17.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   Name=cfiB {ECO:0000313|EMBL:CUH44329.1};
GN   ORFNames=RUM4293_03230 {ECO:0000313|EMBL:CUH44329.1};
OS   Ruegeria atlantica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=81569 {ECO:0000313|EMBL:CUH44329.1, ECO:0000313|Proteomes:UP000050786};
RN   [1] {ECO:0000313|EMBL:CUH44329.1, ECO:0000313|Proteomes:UP000050786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 4293 {ECO:0000313|EMBL:CUH44329.1,
RC   ECO:0000313|Proteomes:UP000050786};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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};
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DR   EMBL; CYPS01000046; CUH44329.1; -; Genomic_DNA.
DR   RefSeq; WP_058274321.1; NZ_CYPS01000046.1.
DR   EnsemblBacteria; CUH44329; CUH44329; RUM4293_03230.
DR   Proteomes; UP000050786; 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; PS00866; CPSASE_1; 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   Complete proteome {ECO:0000313|Proteomes:UP000050786};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:CUH44329.1};
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}.
FT   DOMAIN        3    456       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      123    321       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      533    800       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1070   1145       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   REGION      481    510       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0P1E699}.
FT   COMPBIAS    481    499       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0P1E699}.
FT   ACT_SITE    296    296       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       542    542       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       710    710       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       739    739       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       741    741       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     119    119       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     203    203       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     614    614       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     874    874       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1145 AA;  126377 MW;  2BCF08A25D8A0747 CRC64;
     MTEFTKILIA NRGEIAIRVM RAANEMGKRT VAVFAEEDKL GLHRFKADEA YRIGEGMGPV
     AAYLSIDEII RVAKECGADA IHPGYGLLSE NPDFVDACVQ NGITFIGPKA ETMRALGDKA
     SARRVAVAAG VPVIPATEVL GDDMDAIRAE AKEIGYPLML KASWGGGGRG MRPILSEDEL
     EEMVLEGRRE AEAAFGNGEG YLEKMIIRAR HVEVQILGDK HGEIYHLYER DCSVQRRNQK
     VVERAPAPYL SEEQRAEICE LGRKICAHVN YECAGTVEFL MDMETGKFYF IEVNPRVQVE
     HTVTEEVTGI DIVQAQILIA EGKTLAEATG ANSQSDVHLT GHALQTRITT EDPQNNFIPD
     YGRITAYRSA TGMGIRLDGG TAYAGGVITR YYDSLLTKVT AKAPTPEAAI ARMDRALREF
     RIRGVSTNID FVINLLKHPT FLSNEYTTKF IDTTPDLFSF KRRRDRGTKV LTYIADITVN
     GHPETKDRPE PRADLKDAKP PAPNSEPQMG ARNLLEQKGP QAVADWMKAQ RQLLITDTTM
     RDGHQSLLAT RMRSIDMIKV APTYAANLPQ LFSIECWGGA TFDVAYRFLQ ECPWQRLRNL
     REAMPNLMTQ MLLRGANGVG YTNYPDNVVQ EFVRQASQNI DVFRVFDSLN WVENMRVAMD
     AVVENGKICE GTVCYTGDIL DPDRAKYDLK YYVGMAKELR DAGAHVLGLK DMAGLLKPAS
     AKILIRALKE EVGLPIHFHT HDTAGIASAT ILAASEAGVD AVDCAMDSFS GNTSQATLGT
     VVEALRHTER DTGLDIKAIR EISDYFEAVR GQYAAFESSL QAPASEVYLH EMPGGQFTNL
     KAQARSLGLE ERWHEVAQMY ADVNRMFGDI VKVTPSSKVV GDMALMMVSQ NMTREQVENP
     DTDVAFPDSV VDMMRGNLGQ PPGGFPDTIV TKVLKDETPN TDRPGKDVPP VDLEGTRAEL
     SQLLEGKEVD DEDLNGYLMY PKVFLDYMGR HRVYGPVRTL PTRTFFYGME PGEEITAEID
     PGKTLEIRCQ AIGETDEKGE VKVFFELNGQ PRVIRIPNRL VTSTTQSRPK AEAGNPNHIG
     APMPGVVATV AVAAGQEVKE GDMLLTIEAM KMETGIHAER DATVKAVHVQ PGSQIDAKDL
     LVELE
//
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