ID A0A0M2RAT8_9ACTN Unreviewed; 374 AA.
AC A0A0M2RAT8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
DE Flags: Fragment;
GN ORFNames=LQ51_30700 {ECO:0000313|EMBL:KKJ93254.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ93254.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKJ93254.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKJ93254.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KKJ93254.1}.
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DR EMBL; JTGL01000270; KKJ93254.1; -; Genomic_DNA.
DR RefSeq; WP_046564366.1; NZ_KQ058756.1.
DR AlphaFoldDB; A0A0M2RAT8; -.
DR STRING; 1538294.LQ51_30700; -.
DR HOGENOM; CLU_000395_3_2_11; -.
DR OrthoDB; 249215at2; -.
DR Proteomes; UP000034330; Unassembled WGS sequence.
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 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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKJ93254.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KKJ93254.1}.
FT DOMAIN 1..374
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 346..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 374
FT /evidence="ECO:0000313|EMBL:KKJ93254.1"
SQ SEQUENCE 374 AA; 40003 MW; 5E19AEB2460B89BB CRC64;
MFEKVLIANR GEIALRVLRA CRELGVRTVV VHSSADADSL PVRLADETVR IGPAASRQSY
LNAAAIVEAA RQTGAQAVHP GYGFLSEDAD FAEICAENGL TFVGPSPQVM AALADKSTAR
ELMSEAGLPL PPGSVRTLPT AAEALEVAAG IGYPVIIKAA AGGGGRGMSV VRSAVELPRA
YARTRAAAQV AFGDDRVYVE RYLTDARHVE VQVLCDAHGN GIHLGTRDCS VQRRHQKLIE
EAPAPALRPA TLDALAETAL RGALAVGFTG AGTFEFLVDA AEECHFLEIN CRIQVEHPVT
ELITGLDLVH EQLHIAAGTP LRWRQEQIRP RGVAIEARIN VEDPDRDFAP APGRLDRFRP
PGGPFTRVDT HGHP
//
