ID   A0A1T4Z2P5_9ACTN        Unreviewed;       590 AA.
AC   A0A1T4Z2P5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=biotin carboxylase {ECO:0000256|ARBA:ARBA00013263};
DE            EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263};
GN   ORFNames=SAMN06295964_2115 {ECO:0000313|EMBL:SKB08327.1};
OS   Aeromicrobium choanae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736691 {ECO:0000313|EMBL:SKB08327.1, ECO:0000313|Proteomes:UP000191040};
RN   [1] {ECO:0000313|EMBL:SKB08327.1, ECO:0000313|Proteomes:UP000191040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9H-4 {ECO:0000313|EMBL:SKB08327.1,
RC   ECO:0000313|Proteomes:UP000191040};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; LT796768; SKB08327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4Z2P5; -.
DR   STRING; 1736691.SAMN06295964_2115; -.
DR   Proteomes; UP000191040; 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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          4..447
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          125..320
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          513..589
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   590 AA;  62349 MW;  0FA39D45CB3D7C5A CRC64;
     MSKPLQKVLV ANRGEIAVRV IRAAKDSGIA SVAVYAEPDR DALFVRLADE AYSLEGSTPG
     DSYLSIEKII AIAERSGADS VHPGYGFLAE NADFAQAVID AGLIWIGPPP AAITSLGDKA
     KAKHIAQIAD APLAPGTKDP VKDADEVVAF AKEYGLPVAI KAVFGGGGRG LKVAKTLEEI
     PEAYESAVRE AVSAFGRGEC LVEKFLDKPR HVETQCLADS HGNVVVVSTR DCSLQRRHQK
     LVEEAPAPFL SEDQIASLYA SSKAILKEAG YVGAGTCEFL VARDGTISFL EVNTRLQVEH
     PVSEEVTGID LVREMFRIAA GEELGYDDPE IIGHSIEFRI NAEDGGRGFL PAPGTLTKWA
     PPSGPGVRLD AGYEEGETIP GAFDSLVAKL IVTGRTREQA IERSRRALDE FVVEGMPTVI
     PFHRDVLDNA AYNALNKDGS EGSFDVYTTW IETDYDNQLE PYSGPSETDE PGERERVTVE
     VGGKRVEVVL PGGLGASAAA TGTKKAKRKA GKSAGAAASG DSLTSPMQGT VVKLAVEEGQ
     EVAEGDLVLV IEAMKMEQPI NAHKAGTVTG LSAAIGETVG AGAVICDLKD
//