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
//