ID A0A1C4Y1F0_9ACTN Unreviewed; 480 AA.
AC A0A1C4Y1F0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN ORFNames=GA0070612_4179 {ECO:0000313|EMBL:SCF14533.1};
OS Micromonospora chokoriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=356851 {ECO:0000313|EMBL:SCF14533.1, ECO:0000313|Proteomes:UP000198224};
RN [1] {ECO:0000313|EMBL:SCF14533.1, ECO:0000313|Proteomes:UP000198224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45160 {ECO:0000313|EMBL:SCF14533.1,
RC ECO:0000313|Proteomes:UP000198224};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LT607409; SCF14533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4Y1F0; -.
DR eggNOG; COG0439; Bacteria.
DR Proteomes; UP000198224; Chromosome i.
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 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.
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..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 449..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 51254 MW; D8E37542A0459C60 CRC64;
MFETVLIANR GEIALRVLRA CRELGVRTAV VYSAADADSA AVRHADQAIR IGPASSRRSY
LNAAAIVEAA RQVGAQAVHP GYGFLSEDAD FAEICADNGL TFIGPPPAVM AALADKSSAR
ALMSRAGLPL SPGSVAPVPT AAAAAEIAEA VGYPVIVKAA AGGGGRGMTV VRTPGELRRA
YTRTRAAAQA AFGDDRVYVE RYLTEARHVE VQVLCDSHGN GVHLGTRDCS VQRRHQKLIE
EAPAPALPAA VLDTIAETAL RGALEVGFVG AGTLEFLVDA EEQFHFLEIN CRIQVEHPVT
EMVTGIDLVH EQLHIAAGVP LRWRQEEIRL RGVAVECRVN TEDPGRGFVP TPGRLDRFTP
PGGPFTRVDT HASAGYVIGP WYDSLLAKVI VWAPDRELAL NRLERALDEF DVAGPGMHTT
IPFVRRVLDD AAFRKGRYTT GLVDRLLGVP GAAPAQRPTA TPAPRPASAA TPDVPNRRTR
//
