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Database: UniProt
Entry: A0A1Q5KJM2_9ACTN
LinkDB: A0A1Q5KJM2_9ACTN
Original site: A0A1Q5KJM2_9ACTN 
ID   A0A1Q5KJM2_9ACTN        Unreviewed;       419 AA.
AC   A0A1Q5KJM2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:OKJ81773.1};
GN   ORFNames=AMK32_20445 {ECO:0000313|EMBL:OKJ81773.1};
OS   Streptomyces sp. CB01883.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ81773.1, ECO:0000313|Proteomes:UP000186398};
RN   [1] {ECO:0000313|EMBL:OKJ81773.1, ECO:0000313|Proteomes:UP000186398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01883 {ECO:0000313|EMBL:OKJ81773.1,
RC   ECO:0000313|Proteomes:UP000186398};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKJ81773.1}.
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DR   EMBL; LIWA01000004; OKJ81773.1; -; Genomic_DNA.
DR   RefSeq; WP_073894684.1; NZ_LIWA01000004.1.
DR   AlphaFoldDB; A0A1Q5KJM2; -.
DR   OrthoDB; 24041at2; -.
DR   Proteomes; UP000186398; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR041472; BL00235/CARNS1_N.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR040570; LAL_C2.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF13535; ATP-grasp_4; 1.
DR   Pfam; PF18130; ATPgrasp_N; 1.
DR   Pfam; PF18603; LAL_C2; 1.
DR   SMART; SM01209; GARS_A; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 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:UP000186398}.
FT   DOMAIN          116..311
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   419 AA;  42714 MW;  D61745805F21D7FC CRC64;
     MNTPLLLFVE SNTTGTGRQF AQRARALGAE PVLLSADPGR YPYAAEDELR TVVVDTADGD
     ALWAAVQRLA AGQRIAGVLS SSEYYVATAA DLAARLGLPG PSADAVRACR DKSVQRRTLA
     EAGVPVPWFS VAGEVAEAVA AAQWRGGPVV VKPVQGSGSL GVRLCRDTGE VAAHARGLLA
     ATVNERGLST PARVLVEQYL TGPEFSVEVF GEHAVVTVAK HVGAPPAFVE IGHDVPAVPA
     AADAAALVDS AVHAVKALGL GWGAAHVELR LDAGVARVIE VNPRLAGGMI PELVRRARGV
     DLVGAQVRAG LGLPVDLTDA AGAAGAASIR FLTAGTDAVL GDTDAAEAAA RAVPGVVDAA
     LYRTPGTRVG PAEDFRGRLG HVITAGATPR ESARAADTAL SFGLATALEH APAREAMPV
//
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