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Entry: A0A1B9Y2W7_9FLAO
LinkDB: A0A1B9Y2W7_9FLAO
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ID   A0A1B9Y2W7_9FLAO        Unreviewed;      1150 AA.
AC   A0A1B9Y2W7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=BA195_05565 {ECO:0000313|EMBL:OCK44154.1};
OS   Tenacibaculum soleae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK44154.1, ECO:0000313|Proteomes:UP000093186};
RN   [1] {ECO:0000313|EMBL:OCK44154.1, ECO:0000313|Proteomes:UP000093186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK44154.1,
RC   ECO:0000313|Proteomes:UP000093186};
RA   Eisen J.A., Coil D.A., Lujan K.M.;
RT   "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL   Submitted (JUN-2016) 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   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742}.
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:OCK44154.1}.
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DR   EMBL; MAKX01000001; OCK44154.1; -; Genomic_DNA.
DR   RefSeq; WP_068703252.1; NZ_MAKX01000001.1.
DR   AlphaFoldDB; A0A1B9Y2W7; -.
DR   STRING; 447689.BA195_05565; -.
DR   OrthoDB; 9807469at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000093186; 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: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; 1.10.472.90; Conserved carboxylase domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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:OCK44154.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093186}.
FT   DOMAIN          2..455
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          122..319
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   DOMAIN          1081..1150
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         202
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         1116
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1150 AA;  129121 MW;  F500E1E5404DDE02 CRC64;
     MKIKKVLVAN RGEIAIRIFR ACTEINVKTV GVYTFEDRYS LHRYKADESY QIGENNEPLK
     PYLNIDELIR VALESGVDAI HPGYGFLSEN ANLAQKCEDN GIVFIGPKVS VLKSLGDKIT
     AKKVAVANNI PIIRSNENPL VDIETALSEA EKIGYPIMLK AASGGGGRGM RVIRNDDELK
     KAFVESKREA LNAFGDDTVF LEKYVENPKH IEIQIVADNF GNTVHLFERD CSVQRRYQKV
     IEFAPSFDLN QDTKDALYKY AINICKAVNY NNIGTVEFLV DDDGSIYFIE VNPRVQVEHT
     VTEVVTNIDL IKTQLFIAGG YKLADQQIKI PNQEAVKVNG YALQCRITTE DPQNDFKPDY
     GEITTYRSAS GFGIRLDAGS VYQGAIISPF FDSMLVKVTA NSRTLDGACR KVRRALAEFR
     IRGVKTNMPF LDNILKHDTF RKGAVTVNFI KQNPDLFNFK APRNRATKLV TYLGDVIVNG
     NSDVKKIDTT KTFVKPIVPK FDANAAYPKG TKDLLTELGP DKFSQWLKNE KKVHFTDTTM
     RDAHQSLLAT RMRTYDMLKV AEGYAKNNPN IFSMEVWGGA TFDVCMRFLQ ENPWERLQLL
     RKAMPNVLLQ MLLRGSNGVG YKAYSDNLIE SFVQQSWENG VDIFRIFDSL NWMKSIAPCI
     EHVRNKTQGL AEASICYTGD ILNPKNTKYN LKYYTSLAKD IENAGAHILA IKDMAGLLKP
     YAAYELVSAL KEEINIPIHL HTHDTSSIQS ATYLKAIEAG VDVVDVALGG LSGLTSQPNF
     NSVAEMMKFN ERENDLNIDS LNEYSNYWGA VREYYYPFES GLKAGSGEVF KHEIPGGQYS
     NLKPQAQALG LEDRFHEITK MYGDVNLLFG DIVKVTPSSK VVGDMAQYLV SNNLTVQDVL
     ERGDTISFPQ SVVSFFKGDL GQPVGGFPKD LQKLILKDDT PYTDRPNAHI APLDIEAEYE
     DFKKIFENDL SRPIDFTDFL SYKLYPKVFT EAYNKHLKYD SLLNLPTKNF FYGMERGEEI
     IVELDKGKTL LITLDSVGRP NEDGMVKVYF KVNGQGRTVL IKDESIKIDK VAHVKANKSE
     PKEIGAPLQG MLSTILVKKG EKVSKNQPLF IIEAMKMETT ITANEEGVVQ ELILKAGIMV
     NSEDLVLKLT
//
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