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Database: UniProt
Entry: A0A0C1DIF1_9FLAO
LinkDB: A0A0C1DIF1_9FLAO
Original site: A0A0C1DIF1_9FLAO 
ID   A0A0C1DIF1_9FLAO        Unreviewed;      1145 AA.
AC   A0A0C1DIF1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ORFNames=OA93_21810 {ECO:0000313|EMBL:KIA93640.1};
OS   Flavobacterium sp. KMS.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1566023 {ECO:0000313|EMBL:KIA93640.1, ECO:0000313|Proteomes:UP000031466};
RN   [1] {ECO:0000313|EMBL:KIA93640.1, ECO:0000313|Proteomes:UP000031466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:KIA93640.1,
RC   ECO:0000313|Proteomes:UP000031466};
RA   Smith A.K., Newman J.;
RT   "Flavobacterium sp. KMS.";
RL   Submitted (OCT-2014) 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 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIA93640.1}.
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DR   EMBL; JSYP01000028; KIA93640.1; -; Genomic_DNA.
DR   RefSeq; WP_039116217.1; NZ_JSYP01000028.1.
DR   AlphaFoldDB; A0A0C1DIF1; -.
DR   STRING; 1566023.OA93_21810; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000031466; Unassembled WGS sequence.
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:InterPro.
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; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
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; 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|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:KIA93640.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031466}.
FT   DOMAIN          3..456
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          123..320
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          533..802
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   ACT_SITE        295
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         712
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         741
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         743
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         876
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         712
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1110
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1145 AA;  128126 MW;  06BE92045233DE94 CRC64;
     MRTISKLLVA NRGEIALRIF RAAAELKIKT VAIYTYEDRY SLHRYKADEA YQIGKDTDPL
     KPYLDIDEII KVAKAEGIDA IHPGYGFLSE NVLFATKCAE NGILWIGPNP EVMEQLGDKV
     AAKKIALAAN VPLIEDSKID LSSFSIAQEE ANRIGYPLML KAAAGGGGRG MRVVRKANQL
     EALFNEAKRE AKTAFGDDTL FLEKFIENPK HIEVQLLGDN YGNIVHLFER DCSVQRRFQK
     VVEIAPAPNL KQETKDKLYK YALSIATKVN YNNAGTVEFL VDAAENIYFI EVNPRIQVEH
     TVTEEVTGID IVRSQILIAC GHKLSSPGIY IMGQESLKCS GFAIQCRITT EDPANDFTPD
     YGTIIAYRNA GGYGIRIDEG SSYSGVKISP FFDSMLVKIT ARGRTLEGTS QRLLRTLKEF
     TIEGVKTNIP FLENLIVHPD FQAGNITVNF IGDNPSLMKI KRKSDNVTKN LAFIGNIIVN
     GNADVPFIVP DKKFLTPKLP IPSSAFHDNG TKQLLDQLKP KGFSNWIKEQ KQILYTDCTM
     RDAHQSLLAT RVRTIDMMPF AETFTKDFPQ MFSMEVWGGA TFDVAMRFLN ECPWSRLEQM
     RKAMPNVLLQ MLIRGSNGVG YTAYPDNLVE KFIEVSAQKG IDVFRIFDSL NSIDNMKNSI
     NAVLTNTDSL AEVCMGYSGD ILNPERPKFN LNYYLDLAKR IEDTGAHILC IKDMAGLLKP
     YAAEKLITEL KKSIDIPIHL HTHDTAGIQS ATYLKAVEVG VDIIDVALSS MSGLTSQPNF
     NVFAEALKGT PRDSGLDVEK LNQYSNYWED IREYYYPFES DLKSSTAEVY KHEIPGGQYS
     NLKPQAYSLG LETRMTAIKQ AYQDANSLLG DIIKVTPSSK VVGDLAMFMV SSNLSKQDVL
     DQGTTLSFPN SVKGMLKGEL GQPDGGWPID FQQMVLKKEK PFLDLPNAHL TPIDFDNEFE
     AFQEKFSSSC TLADFISYQF YPKVFEDYFK TIEKYGDVSV IPSTTFFYGL KPNEEVIVNI
     SEGKSIIVKF LYKSEPDLQG IRTVYFKLNG QTKAIEIKDK SIKTMNVQNR KALTAAEIGA
     PLPGLLSKIW IKEGEEIKQD QPLFTIEAMK MENTVLGKSG IIHKIHLNEN SLVEKGDLLI
     EYLVE
//
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