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Database: UniProt
Entry: A0A3N5AK99_9ACTN
LinkDB: A0A3N5AK99_9ACTN
Original site: A0A3N5AK99_9ACTN 
ID   A0A3N5AK99_9ACTN        Unreviewed;       410 AA.
AC   A0A3N5AK99;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   05-FEB-2025, entry version 17.
DE   SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:RPF44220.1};
GN   ORFNames=EDD96_0741 {ECO:0000313|EMBL:RPF44220.1};
OS   Streptomyces sp. Ag109_G2-6.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2485154 {ECO:0000313|EMBL:RPF44220.1, ECO:0000313|Proteomes:UP000277533};
RN   [1] {ECO:0000313|EMBL:RPF44220.1, ECO:0000313|Proteomes:UP000277533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ag109_G2-6 {ECO:0000313|EMBL:RPF44220.1,
RC   ECO:0000313|Proteomes:UP000277533};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (NOV-2018) 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:RPF44220.1}.
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DR   EMBL; RKRC01000001; RPF44220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N5AK99; -.
DR   Proteomes; UP000277533; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR052032; ATP-dep_AA_Ligase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; 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.
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:UP000277533}.
FT   DOMAIN          110..308
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   410 AA;  44069 MW;  81073B892065499A CRC64;
     MTDRLLVCGL GSGMDRSLTE LRSPRWELVV ATDRPTDRAR AAADVLLAVD PNDAVAVLAE
     LSAAGIDRID GVFSLGADNP PVISTLARRF GCPGLPLETA LDCTLKDRRL RILRAAGLDL
     PRFATAESVG EAVRAAADIG LPVVLKPSDQ TGSLGVLKAE SAGQVRALAQ EALRLSPGGR
     IVVEEFLEGT EHTLAAFMVD GALHRFGFAD REYGNKERFA PHFFEGGDTL PSRLTDEQIE
     EVTETVRRGA TALRLDPAVV NTDILRTRDG RVVLLEITCR LTGARIATEV MRLATGVDPL
     PNVVRLALGR PLDLAELRPR HSRAAVQRFL PADGGVVEWA GDPRDVARRA GVHDVFWGLD
     LRPGTVVPPY RGGAEVLAGV IAHAERPQEA EAIAERTLNS LPLRFKAGTQ
//
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