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Database: UniProt
Entry: A0A1C5HVB4_9ACTN
LinkDB: A0A1C5HVB4_9ACTN
Original site: A0A1C5HVB4_9ACTN 
ID   A0A1C5HVB4_9ACTN        Unreviewed;       445 AA.
AC   A0A1C5HVB4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=GA0070613_1827 {ECO:0000313|EMBL:SCG49561.1};
OS   Micromonospora inositola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG49561.1, ECO:0000313|Proteomes:UP000198221};
RN   [1] {ECO:0000313|EMBL:SCG49561.1, ECO:0000313|Proteomes:UP000198221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG49561.1,
RC   ECO:0000313|Proteomes:UP000198221};
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; LT607754; SCG49561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5HVB4; -.
DR   OrthoDB; 249215at2; -.
DR   Proteomes; UP000198221; 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.
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:UP000198221}.
FT   DOMAIN          1..445
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   445 AA;  47187 MW;  50741C5FE7A52BD2 CRC64;
     MIESLLVANR GEIARRIIRT AKRLGIRAIA VHSEADAGLP FVTEADEAVN IGPANPAQSY
     RNVEAILAAA KSTGAQAIHP GYGFLSENAD FARTVEASGL IWVGPGADAI TAMGDKINAR
     NLMAAAGVPV APGTTDPAAD LAAAVAAGAE IGYPVMVKAA AGGGGMGMGV ATDEAALRTE
     YDKVRSFAER MFGDGSVLIE RYFPRVRHVE VQILGLADGR VVALGERECS VQRRNQKLVE
     ESPSPAVSPE LRERFLAAAV RAGEAVGYRN AGTVECLLDP ATNEFFFLEM NTRLQVEHPV
     TELVYGVDLV EEQLRVAAGL APTFDPDALA PRGHAIELRI NAEDPKRFLP GPGAIATWNE
     PTGSGVRVDS GYVAGNTVTP FYDSLMAKLI VSGRDRAEAV ERAKAAVAQF EIAGPKCNLP
     FFAELLENEE FLSGDYDTGI VGRMR
//
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