ID M1PJ39_DESSD Unreviewed; 701 AA.
AC M1PJ39;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:AGF79590.1};
GN OrderedLocusNames=UWK_03061 {ECO:0000313|EMBL:AGF79590.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79590.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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; CP003985; AGF79590.1; -; Genomic_DNA.
DR RefSeq; WP_015405274.1; NC_020304.1.
DR AlphaFoldDB; M1PJ39; -.
DR STRING; 1167006.UWK_03061; -.
DR KEGG; dsf:UWK_03061; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_393169_0_0_7; -.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000011721; 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 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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; PF00289; Biotin_carb_N; 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 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT DOMAIN 61..547
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 192..395
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 701 AA; 79610 MW; 7AC6DF281264F925 CRC64;
MLLNGTSEAE QGKTVYLEKI CEISSRLVIG INSIFVRKMN DKPLLSACEN KLVEGKYLQE
DFQYVLIWNR GVIASMVAEQ AYEVGKKVIF VHDGKDARPD RSDGDLIFTA PYSATPEQKG
RGDRPDITAL DQLLLFLKNH NIPLDQIVLH PGYGFNSEDP VFFEALEKRE IRFLGAGSKH
IDFIGNKVNA NKIAAQTSIK PPGSSGRIET VNQALTFFQL CHKDGIQKIV LKDAYGGGGS
GQKLIAVDDP QAENIIVQTV NEWLDKGTTF SIDQWIEKSR HIEMQVMVDQ GGNVRFGSPR
DCTMQRAKQK IIEETASITL SQELQLRESI QDYFKMVEEK LEKPYVGLAT FEMLYEPDTG
NFNFLEVNTR IQVEHPVSGH QGGIQFIRTQ FDIASGQRLH DQEKLDRRRD KVGGHTIEAR
ICLEEVLETG MIQFVKEMLH KDALTLGVSG KVAIRLPERA NSTFYFDNRI IRDREVANGQ
GRYDTMVGQV VSRGVDRKSA IFELEMAVKS LQIKGVSSNI ELVATILDDP EFRDDRHSSR
SSVVDRFMEK KIAEKDLLEE NKKKRQIALN KFKDEPEQVG IADLVRVIDL PLAPCRTTVK
NIIDFFTPPG SAFQAKSFEK RYFLVETSLV NRDLFRFLSC FQVTSADAYI ASDIKLFAIP
TCMENPFRLF WQYYTGENPF EVKQCLLRSQ NLQFFCMKTN N
//
