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Database: UniProt
Entry: A0A0Q0YKA0_9CORY
LinkDB: A0A0Q0YKA0_9CORY
Original site: A0A0Q0YKA0_9CORY 
ID   A0A0Q0YKA0_9CORY        Unreviewed;       576 AA.
AC   A0A0Q0YKA0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:KQB87285.1};
DE            EC=6.2.1.3 {ECO:0000313|EMBL:KQB87285.1};
GN   Name=fadD {ECO:0000313|EMBL:KQB87285.1};
GN   ORFNames=Clow_00340 {ECO:0000313|EMBL:KQB87285.1};
OS   Corynebacterium lowii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1544413 {ECO:0000313|EMBL:KQB87285.1, ECO:0000313|Proteomes:UP000050488};
RN   [1] {ECO:0000313|EMBL:KQB87285.1, ECO:0000313|Proteomes:UP000050488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 130206 {ECO:0000313|EMBL:KQB87285.1,
RC   ECO:0000313|Proteomes:UP000050488};
RA   Bernard K., Pacheco A.L., Mcdougall C., Burtx T., Weibe D., Tyler S.,
RA   Olson A.B., Cnockaert M., Eguchi H., Kuwahara T., Nakayama-Imaohji H.,
RA   Boudewijins M., Van Hoecke F., Bernier A.-M., Vandamme P.;
RT   "Corynebacteirum lowii and Corynebacterium oculi species nova, derived from
RT   human clinical disease and and emended description of Corynebacterium
RT   mastiditis.";
RL   Submitted (OCT-2015) 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:KQB87285.1}.
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DR   EMBL; LKEV01000001; KQB87285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q0YKA0; -.
DR   STRING; 1544413.Clow_00340; -.
DR   PATRIC; fig|1544413.3.peg.343; -.
DR   Proteomes; UP000050488; Unassembled WGS sequence.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   CDD; cd05936; FC-FACS_FadD_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43767:SF12; AMP-DEPENDENT SYNTHETASE AND LIGASE; 1.
DR   PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:KQB87285.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050488}.
FT   DOMAIN          40..433
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          483..558
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   576 AA;  63249 MW;  D303B9A7F50499B4 CRC64;
     MPEGSPVSAA EERAWLKHYP EWTPHHLDYG DTTLLDVYDH TLATKPEKPA TWFFGRSQSY
     SDIDEQVRAA AAGLRALGVR PGDRVAVALP NCPQHIVIFY AILKLGAAVV EHNPLYTAHE
     LEVPFRDHGA RVAITWDKSA DVFEKLRSST DLETIISVNM VNAMPPLKRL ALRLPLPKVK
     KMRAQLTSPA PNTIPWDLLL SPQLGGNGSD VTSLETVDKD TPALVLYTSG TTGTPKGAQL
     THGNLYANIL QGKAWVPGLG DQDERMLAAL PMFHAYGLTM NATLGFLIGG ELMLLPSPET
     SLLMDVMKNH TPTWVPGVPT LYEKIVEAAA EDDITIKGVR SSFSGASTLP ISTVERWESM
     TGGLLVEGYG LTETSPIIVG NPMSTARRPG YVGIPFPDTD VRIADPNDLS RTMPDGEEGE
     VLVRGPQVFH GYLNNPEATE KSFYEGWYRT GDVGVMEEDG FIRLVARIKE VIITGGFNVY
     PSEVEEVMRE HSDIADVAVV GVPRQDGSES VVACITLNPG AALDPEGLKQ FAREHLTRYK
     VPRTFYHFEE LARDQMGKIR RRQVQADLLE HLGIKG
//
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