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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//