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Database: UniProt
Entry: A0A0P1GU35_9RHOB
LinkDB: A0A0P1GU35_9RHOB
Original site: A0A0P1GU35_9RHOB 
ID   A0A0P1GU35_9RHOB        Unreviewed;      1147 AA.
AC   A0A0P1GU35;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-DEC-2018, entry version 15.
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:CUH86460.1};
GN   ORFNames=PH5382_00369 {ECO:0000313|EMBL:CUH86460.1};
OS   Phaeobacter sp. CECT 5382.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH86460.1, ECO:0000313|Proteomes:UP000050782};
RN   [1] {ECO:0000313|EMBL:CUH86460.1, ECO:0000313|Proteomes:UP000050782}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH86460.1,
RC   ECO:0000313|Proteomes:UP000050782};
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; CYSG01000001; CUH86460.1; -; Genomic_DNA.
DR   RefSeq; WP_058332614.1; NZ_CYSG01000001.1.
DR   EnsemblBacteria; CUH86460; CUH86460; PH5382_00369.
DR   Proteomes; UP000050782; 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:UP000050782};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:CUH86460.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050782}.
FT   DOMAIN        3    456       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      123    321       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      534    802       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1072   1147       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    296    296       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       543    543       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       712    712       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       741    741       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       743    743       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     615    615       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     876    876       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1147 AA;  126133 MW;  105EE12F5856F084 CRC64;
     MTDFKKILIA NRGEIAIRVM RAANEMGKRT VAVYAEEDKL GLHRFKADEA YRIGEGMGPV
     AAYLSIDEII RVAKECGADA IHPGYGLLSE NPDFVDACAR NGITFIGPKA ETMRALGDKA
     SARRVAVEAG VPVIPATEVL GSDMAAIKAE ASEVGYPLML KASWGGGGRG MRPIYSEEEV
     EEKVLEGRRE AEAAFGNGEG YLEKMITRAR HVEVQILGDK HGEIYHLFER DCSVQRRNQK
     VVERAPAPYL SEEQRAEICD LGRKICQHVN YECAGTVEFL MDMETEKFYF IEVNPRVQVE
     HTVTEEVTGI DIVQAQILIA EGKTIAEATG KASQDEIRLN GHALQTRVTT EDPLNNFIPD
     YGRITAYRSA TGMGIRLDGG TAYAGGVITR YYDSLLTKVT AWAPTPEKAI ARMDRALREF
     RVRGVSTNIA FVENLLKHPT FLDNSYTTTF IDNTPALFQF AKRQDRGTKV LTYLADISVN
     GHPETEGRAA PAADLKEPRA PHVEPGQTPY GTRNLLEQKG AQAVADWMKA QRQLLLTDTT
     MRDGHQSLLA TRMRSHDMIK VAPAYAQNLS QLFSVECWGG ATFDVAYRFL QECPWQRLRD
     LREAMPNVMT QMLLRASNGV GYTNYPDNVV QEFVRQAAVT GVDVFRVFDS LNWVENMRVA
     MDAVVESGKL CEGTICYTGD ILDPNRAKYD LKYYIGMAKE LEAAGAHILG LKDMAGLLKP
     AAARQLVKAL KEEVGLPVHF HTHDTSGIAG ATILAAADAG VDAVDVAMDA FSGGTSQPCF
     GSIVEGLRNT DRDTGLDIAK IREISDYWEQ VRAQYAAFES GLQAPASEVY LHEMPGGQFT
     NLKAQARSLG LEERWHEVAQ TYADVNQMFG DIVKVTPSSK VVGDMALMMV SQNLTRDEVE
     DPETDVSFPD SVVDMMRGNL GQPPGGFPDS IVAKVLKGEA PNLTRPGAHL APVDLDETRA
     ELSQMLEGKS VDDEDLNGYL MYPKVFLDYM GRHRQYGPVR TLPTRAFFYG MEPGEEITAE
     IDPGKTLEIR LQALGETDET GEVKVFFELN GQPRVIRVPN RLVKASTESR PKAEAGNPDH
     IGAPMPGVVA SVAVHVGQEV HEGDMLLTIE AMKMETGLHA ERSATVKALH VAAGTQIDAK
     DLLIEFE
//
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