ID W0BCK2_9GAMM Unreviewed; 278 AA.
AC W0BCK2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:AHE66342.1};
GN ORFNames=Loa_00774 {ECO:0000313|EMBL:AHE66342.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE66342.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE66342.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
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DR EMBL; CP004006; AHE66342.1; -; Genomic_DNA.
DR AlphaFoldDB; W0BCK2; -.
DR STRING; 1268635.Loa_00774; -.
DR KEGG; lok:Loa_00774; -.
DR PATRIC; fig|1268635.3.peg.774; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_4_6; -.
DR Proteomes; UP000018838; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 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; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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 Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000018838}.
FT DOMAIN 1..277
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 30..149
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 278 AA; 31607 MW; 5B86510B79B27DF0 CRC64;
MRVVHTEANL LNAIALTRSE AKAAFNNPVV YMEKFLENPR HIEFQVLGDG KGNAVHLGER
DCSMQRRHQK VIEEAPAPGI TPALRQEIGE RVVNACRELN YRGAGTFEFL YQDGCFYFIE
MNTRIQVEHP VTELITGIDL IKEQIKIASD IPFTLTQENI KWHGHAVECR INAEDPKTFM
PSPGTIRLLH QPGGPGIRFD SHIYSSYTVP PNYDSMIGKL ISYGETRQEA FARMRNALDE
IIIEGIKTNV ELHQRILHDK GFIQGGTNIH YLEKLLKE
//
