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Database: UniProt
Entry: F7ZDF3_ROSLO
LinkDB: F7ZDF3_ROSLO
Original site: F7ZDF3_ROSLO 
ID   F7ZDF3_ROSLO            Unreviewed;      1146 AA.
AC   F7ZDF3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN   Name=pyc {ECO:0000313|EMBL:AEI94555.1};
GN   OrderedLocusNames=RLO149_c025870 {ECO:0000313|EMBL:AEI94555.1};
OS   Roseobacter litoralis (strain ATCC 49566 / DSM 6996 / JCM 21268 / NBRC
OS   15278 / OCh 149).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=391595 {ECO:0000313|EMBL:AEI94555.1, ECO:0000313|Proteomes:UP000001353};
RN   [1] {ECO:0000313|EMBL:AEI94555.1, ECO:0000313|Proteomes:UP000001353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49566 / DSM 6996 / JCM 21268 / NBRC 15278 / OCh 149
RC   {ECO:0000313|Proteomes:UP000001353};
RX   PubMed=21693016; DOI=10.1186/1471-2164-12-324;
RA   Kalhoefer D., Thole S., Voget S., Lehmann R., Liesegang H., Wollher A.,
RA   Daniel R., Simon M., Brinkhoff T.;
RT   "Comparative genome analysis and genome-guided physiological analysis of
RT   Roseobacter litoralis.";
RL   BMC Genomics 12:324-324(2011).
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step and
CC       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(+) + oxaloacetate
CC         + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, 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|ARBA:ARBA00001953,
CC         ECO:0000256|PIRNR:PIRNR001594};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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DR   EMBL; CP002623; AEI94555.1; -; Genomic_DNA.
DR   RefSeq; WP_013962476.1; NC_015730.1.
DR   AlphaFoldDB; F7ZDF3; -.
DR   STRING; 391595.RLO149_c025870; -.
DR   KEGG; rli:RLO149_c025870; -.
DR   eggNOG; COG1038; Bacteria.
DR   HOGENOM; CLU_000395_0_1_5; -.
DR   OMA; YAIQSRV; -.
DR   OrthoDB; 9763189at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001353; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniPathway.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 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   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 2.
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   NCBIfam; TIGR01235; pyruv_carbox; 1.
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   PIRSF; PIRSF001594; Pyruv_carbox; 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; 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:AEI94555.1}.
FT   DOMAIN          3..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          123..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          533..801
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1071..1146
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          481..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         542
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         614
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         711
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         740
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         742
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         875
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         711
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1112
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1146 AA;  126015 MW;  3BCF4E363CB6D61C CRC64;
     MPEFKKILIA NRGEIAIRIM RAANEMGKKT VAVFAEEDKL GLHRFKADEA YRIGEGMGPV
     AAYLSIDEII RVAKEAGADA IHPGYGLLSE NPDFVDACDQ NGIVFIGPRA ETMRALGDKA
     SARRVAVEAG VPVIPATEVL GDDMKAIKAE AKQVGYPLML KASWGGGGRG MRPIQQEDEL
     EEKVLEGRRE AEAAFGNGEG YLEKMILRAR HVEVQILGDK HGDMYHLFER DCSVQRRNQK
     VVERAPAPYL TEAQRAEVCK LGYDICKHVN YECAGTVEFL MDMDDGKFYF IEVNPRVQVE
     HTVTEEVTGI DIVQAQILIA EGKTIAEATG KPTQADVQLT GHALQTRITT EDPQNNFIPD
     YGRITAFREA TGMGIRLDGG TAYSGGVITR YYDSLLVKVT AKAQTPDAAI ARMDRALREF
     RIRGVSTNIA FVENLLKHPT FLNNEYHTKF IDETPELFQF SKRRDRGTKV LTYIADITVN
     GHPETKAHPR PPAHVKDPRA PKERAEPMMG TRNLLEQKGP QGVADWMKQQ RQLLITDTTM
     RDGHQSLLAT RMRSIDMIKV APSYSANLPQ LFSVECWGGA TFDVAYRFLQ ECPWQRLRDL
     RAAMPNLMTQ MLLRASNGVG YTNYPDNVVQ EFVRVAASTG VDVFRVFDSL NWVENMRVAM
     DAVIENGKVC EGSICYTGDI NDPDRAKYNL KYYVDMGKEL RDAGAHVLGL KDMAGLLKPA
     AARQLVRTLK SEVGLPIHFH THDTAGVACA TILAASEAGV DAVDCAMDAL SGNTSQATLG
     SVVSALKHTD RDTGLDMSAI REISDYWEEV RNHYAAFETG MQAPSSEVYL HEMPGGQFTN
     LKAQAASLGL ADRWHEVAQT YAEVNQMFGD IVKVTPSSKV VGDMALMMVS QGLSRADVEN
     PDTDVSFPDS VVDMMRGNLG QPPGGFPEAI VKKVLKDEQP VLDRPGKHLP PADLEALRAE
     ASNLMEGKLV DDEDLSGYLM YPKVFLDYMG RHRTYGPVRA LPTKTFFYGM EPGEEISAEI
     DPGKTLEIRL QTVGDTGEDG EVRVFFELNG QPRVIRVPNR LVAATTQKRP KAETGNAKHI
     GAPMPGVVAS VAAKGGGKVK AGDLLLTIEA MKMETGIHAE KAATVKTVHV SPGGQIDAKD
     LLIEFE
//
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