ID A0A0S8CCC0_9CHLR Unreviewed; 512 AA.
AC A0A0S8CCC0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE RecName: Full=Biotin carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ76_02910 {ECO:0000313|EMBL:KPK21313.1};
OS Dehalococcoidia bacterium SM23_28_1.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703395 {ECO:0000313|EMBL:KPK21313.1, ECO:0000313|Proteomes:UP000054497};
RN [1] {ECO:0000313|EMBL:KPK21313.1, ECO:0000313|Proteomes:UP000054497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_28_1 {ECO:0000313|EMBL:KPK21313.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK21313.1}.
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DR EMBL; LJTZ01000063; KPK21313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CCC0; -.
DR PATRIC; fig|1703395.3.peg.561; -.
DR Proteomes; UP000054497; Unassembled WGS sequence.
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; 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; 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; PS00866; CPSASE_1; 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}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 512 AA; 56349 MW; F72DDE38D3D7F73F CRC64;
MFTKLLVANR GEIALRILRS CRDLGIGGVA VYSEVDRDSL HVRYADEAYL IGPGPATESY
LNGSKILEVA KKARVDAIHP GYGFLAENAG FARACRENGI TFVGPTPESI RLLGDKIKAR
RLMSEAGIPV VPGSRELGTT NMATLAATRI GYPLLVKAAA GGGGKGIRAV YRAEELPIAL
EVAGREAGSA FGDSALYLEK FLETVRHVEV QIIADYHGNV VALGERECSI QRRYQKMIEE
APSTAVDEAL RERLMEMAVK AGAAADYVNV GTVEFLLDEE GNPSFLEVNT RLQVEHPVTE
LVTGVDLVAD QILVAEGERL PYRQEDIRVR GWAIECRIAA EDPFNEFLPS VGRVSFVSEP
GGPGVRVDSA LYNGTNIPHY YDPLIAKLSI RGRDRAEAIR RMRRALQEFK IVGVDTNIPF
HLQVMDNVHF IAGALDTAFV DKHLRFDEQD ELENEQIALV AASLLAHNKK KEALRSSAPA
GVSGGSWRLQ SRRSGLRERD WAMRRMTWRK ST
//
