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Database: UniProt
Entry: E9AZT3_LEIMU
LinkDB: E9AZT3_LEIMU
Original site: E9AZT3_LEIMU 
ID   E9AZT3_LEIMU            Unreviewed;       741 AA.
AC   E9AZT3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative long-chain-fatty-acid-CoA ligase {ECO:0000313|EMBL:CBZ28484.1};
GN   ORFNames=LMXM_28_1150 {ECO:0000313|EMBL:CBZ28484.1};
OS   Leishmania mexicana (strain MHOM/GT/2001/U1103).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=929439 {ECO:0000313|EMBL:CBZ28484.1, ECO:0000313|Proteomes:UP000007259};
RN   [1] {ECO:0000313|Proteomes:UP000007259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHOM/GT/2001/U1103 {ECO:0000313|Proteomes:UP000007259};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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DR   EMBL; FR799581; CBZ28484.1; -; Genomic_DNA.
DR   RefSeq; XP_003876955.1; XM_003876906.1.
DR   AlphaFoldDB; E9AZT3; -.
DR   GeneID; 13450570; -.
DR   KEGG; lmi:LMXM_28_1150; -.
DR   VEuPathDB; TriTrypDB:LmxM.28.1150; -.
DR   OMA; CLMLYTS; -.
DR   OrthoDB; 5473537at2759; -.
DR   PhylomeDB; E9AZT3; -.
DR   Proteomes; UP000007259; Chromosome 28.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05941; MCS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF8; FATTY ACID COA SYNTHETASE FAMILY; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:CBZ28484.1}.
FT   DOMAIN          120..575
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          635..728
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   741 AA;  81791 MW;  76448F255A950EC2 CRC64;
     MFRVFTSPIL AKVPYATLFE YNHVLKKVFE AQPSKVALRH EVPGMPEVQF TYGQLQRDVV
     AMADAMVRRK EAVAQARGET SLSWLQPSRP AHVRSVFAQG ERTPSCDYMK DTGFYTTSVL
     CGPGYTYAVS LLASWSLNQL VTPMSVSQRY KDELMYVLKH SGSRSIVGNT NLLKEKLPAE
     YEELYVRAEV DIDKIPQSAS REPKLPENSS VTSNTFLVDT VYDATLLVRD ITAKRDTKET
     AMLETEWLPP AKSACAPMQS AQDLVKRLDD EKAAAKAREL DRHAEIVQQE HLLRNRAPTE
     ATGGAVPAGS DVDGDGLFCF DSGHLDGLNP VYQRWHAMPW ARPTKYDDCL MLYTSGTTAK
     PKGVVHTHAS VTNMVKVLQD AWQWRDTDSI LHVLPWHHVH GLVNILLCAI ASNARCVVTT
     FDDAARVAHR LEQGDITLFM AVPTVYAKLS DAVQRKFSPV EKTGFRKACM ESVRLMVCGS
     APLPVPTLNQ FCELSGHTLL ERYGMTEIGM ALSQPLHPIS DRHPGTVGSP LPTVKTYVHQ
     PETAEAMEQA SAKEAEYDEV GGLSIASESL FDRYWNNATA TKKEVRTNAA GMRFFDTGDT
     VGVRLRARKP AVYTILGRST VDIIKSRGYK LSALEIEATL LARNDLFYEM AVVGAADAVQ
     GESVVAVVAM QPEAARARGI AFGKGAAWCE SAAVTEELKK VALQLLAPYK CPSRYIVVPE
     IPRNATGKVN KKELKKVLSL P
//
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