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Database: UniProt
Entry: B0SQY4_LEPBP
LinkDB: B0SQY4_LEPBP
Original site: B0SQY4_LEPBP 
ID   B0SQY4_LEPBP            Unreviewed;       917 AA.
AC   B0SQY4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   13-SEP-2023, entry version 88.
DE   SubName: Full=Biotin carboxylase (A subunit of acetyl-CoA carboxylase ACC) {ECO:0000313|EMBL:ABZ97685.1};
DE            EC=6.3.4.14 {ECO:0000313|EMBL:ABZ97685.1};
DE            EC=6.4.1.2 {ECO:0000313|EMBL:ABZ97685.1};
GN   Name=fabG7 {ECO:0000313|EMBL:ABZ97685.1};
GN   OrderedLocusNames=LEPBI_I1578 {ECO:0000313|EMBL:ABZ97685.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97685.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ97685.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP000786; ABZ97685.1; -; Genomic_DNA.
DR   RefSeq; WP_012388564.1; NC_010602.1.
DR   AlphaFoldDB; B0SQY4; -.
DR   SMR; B0SQY4; -.
DR   STRING; 456481.LEPBI_I1578; -.
DR   KEGG; lbi:LEPBI_I1578; -.
DR   HOGENOM; CLU_306483_0_0_12; -.
DR   OMA; FHYGLVN; -.
DR   OrthoDB; 9763189at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS07785-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR48095:SF4; BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding 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; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABZ97685.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          25..590
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          217..447
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          801..890
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   917 AA;  102669 MW;  A12507C875688BCF CRC64;
     MLDKNLKRIQ FQESESAWIR SFTVESIKCL IVCRGPVRKE TMDVFDAIGV KEYGILLSEK
     DSIVYPKALA PELRNFRFPE NIHRVPDYMG AGKEEKELRI HQIIGIAKDN GYTHIFAGYG
     FMAEDAEFIE AIERAGITFM GPSSHVAKGA GAKDEAKKLA RSLNVSVTPG VDNITALALL
     RKTGNSKDGL QKVAKENNLN FSFDEKKSLE DNAEILLQLS YEKTIDITSI PDLQKESEIL
     CEDIWKKYPG KRIRFKYIGG GGGKGQRVIS SKGEIESAVM EILAESKVTA VGSNRNFLIE
     LNIENTRHNE IQLIGNGEWS LSLGGRDCSL QMHEQKLLEI SQTVELLQKE ADLVRSSNSK
     KAAILDNDVQ TLKDMEHQAE VFGKAIKLNS VSTFECIVEG NSFFFMEVNT RIQVEHRVTE
     MVYKMKFTNP NDPNDFFYID SLVEAMAVLS IHGPRVPKPE RIVRNVSGAE VRINATNRAL
     QPHAGGIIQN WSNALPEEIR DDQGICTRNP DTGAFVHYNL AGAYDSNVAL IVSYGNSRTE
     NLEILGNILR KTELRGQNLE TNLLVHYGLI QWILGKDAMF KPSTAFMISY LAGIGALQSI
     INDLDLEYLW SEKTKASDAD LKKILSKKMT LVVRPMERLL ANPHLLGGFL GYFDGKLWTR
     SGNNVSFNEN PIQFLDSLYY YLNLDTTAQK ASSEKIWDHD EKLLIEAKEF YSELSKRTGL
     KTWKEISDVL AKGKNPSKEI SDELWEKVKA SHNGFQAGLE TLLLLPKIGI KSNFFGLDVN
     VDLDGVVPDE FKNKDTRDAF IKTLNPPPKM SGDEIVAPMG GMFYSKEAPN LPPLVNEGDH
     FQAGQPLFII EVMKMFNKIL APVSGTMVKN LMVDSDGKIV TKAQPIFKIK PDEILKEESP
     EDIRARKVKV TKELGLG
//
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