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Database: UniProt
Entry: A5E9V0_BRASB
LinkDB: A5E9V0_BRASB
Original site: A5E9V0_BRASB 
ID   A5E9V0_BRASB            Unreviewed;       651 AA.
AC   A5E9V0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=Putative biotin carboxylase {ECO:0000313|EMBL:ABQ32944.1};
DE            EC=6.3.4.- {ECO:0000313|EMBL:ABQ32944.1};
GN   OrderedLocusNames=BBta_0676 {ECO:0000313|EMBL:ABQ32944.1};
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ32944.1, ECO:0000313|Proteomes:UP000000246};
RN   [1] {ECO:0000313|EMBL:ABQ32944.1, ECO:0000313|Proteomes:UP000000246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP000494; ABQ32944.1; -; Genomic_DNA.
DR   RefSeq; WP_012040995.1; NC_009485.1.
DR   AlphaFoldDB; A5E9V0; -.
DR   STRING; 288000.BBta_0676; -.
DR   KEGG; bbt:BBta_0676; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_5; -.
DR   OMA; VWLGHRD; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000000246; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; 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; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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   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; 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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABQ32944.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          5..448
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          124..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          575..650
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   651 AA;  69015 MW;  594E182EA601A204 CRC64;
     MSRRPFHKVL IANRGEIALR VMRTARRLGH GVVAVYSDAD QDAPHVRLAD QAVRIGAPPP
     AQSYLNIAAI IAAAKATGAD AVHPGYGFLA ENEDFAQACT DAGLVFIGPS PDAIAAMGNK
     AGAKDIMLRA GVPCVPGYQG EDQNDEAMLR EARRIGFPVM IKAVAGGGGR GMRLVSDADA
     FLDMLRSARS EAAAAFGDGT VILEKAIANP RHIEIQVFGD SHGNAVHLGE RDCSVQRRHQ
     KLIEEAPSPA VGPELRARMG AVAVQAVKAL VYEGAGTLEF LLDGDGQFYF MEMNTRLQVE
     HPVTEALTGL DLVEWQLRVA AGEPLPLRQE QIRLEGHAIE VRLCSEDAAQ DFMPQSGRMA
     LWQMPEEIRV EHALESGAEI PPYYDSMIAK LISHGASREE ARARLMVGLE QAAALGVTTN
     QAFLLSCLRH PAFVAGKATT AFIAAHGDDL NAPAVAAADV ALATLVLSVS HPLAHPVGGG
     RSLAASFATP LRFEIGGAVR DAELLRERDG SYRVTCDGTE HGCEVISLSG DMIRVRRGDI
     TESARFVRDG DQLFVQHRGQ TLALRDLTLA APQSSAAAGG DGKVRAALNG RVVAVLVKLG
     DRVAVGQPVI TLEAMKMEHV HAAGLAGTVT AIEVAEGDQV TTGRIVVEIA A
//
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