ID B2HMT7_MYCMM Unreviewed; 549 AA. AC B2HMT7; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 63. DE SubName: Full=Fatty-acid-CoA ligase FadD5 {ECO:0000313|EMBL:ACC38876.1}; GN Name=fadD5 {ECO:0000313|EMBL:ACC38876.1}; GN OrderedLocusNames=MMAR_0409 {ECO:0000313|EMBL:ACC38876.1}; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC38876.1, ECO:0000313|Proteomes:UP000001190}; RN [1] {ECO:0000313|EMBL:ACC38876.1, ECO:0000313|Proteomes:UP000001190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190}; RX PubMed=18403782; DOI=10.1101/gr.075069.107; RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum on the RT evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000854; ACC38876.1; -; Genomic_DNA. DR RefSeq; WP_012392388.1; NC_010612.1. DR AlphaFoldDB; B2HMT7; -. DR STRING; 216594.MMAR_0409; -. DR KEGG; mmi:MMAR_0409; -. DR eggNOG; COG0318; Bacteria. DR HOGENOM; CLU_000022_59_0_11; -. DR OrthoDB; 9803968at2; -. DR Proteomes; UP000001190; Chromosome. DR GO; GO:0016877; F:ligase activity, forming carbon-sulfur bonds; IEA:UniProt. DR CDD; cd17631; FACL_FadD13-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; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1. DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 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:ACC38876.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001190}. FT DOMAIN 31..394 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 444..518 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" SQ SEQUENCE 549 AA; 59547 MW; 68D233C97D0509EF CRC64; MTAELASHLP QAAHALEQPY LARRQNWVNQ LERHAMMQPR ATAIRYLGHT VTWADLRYRV AALAGSLSRR GVGFGDRVMI LMLNRTEFVE SVLAANMLGA IAVPLNFRLT PSEIAFLVED CAPRLVITEE VLAQVAVGVR EIAPALSTIV VAGGASDPTV VGYDELISET GDPPEPVDIP NDSPALIMYT SGTTGRPKGA VLTHTNLTGQ VMTALYTGGA NINSDVGFIG VPFFHIAGIG NMLSGMLLGV PTVIYPLGAF NPGQLLDVLE AERVSGIFLV PAQWQAVCAE QQARPRELSL RVMSWGAAPA PDALLRQMSE VFPGTQIMAA FGQTEMSPVT CMLLGEDAIR KRGSVGKVIP TVSARVVDDE MNDVPIGQVG EIVYRAPTLM SGYWNNPDAT AEAFAGGWFH SGDLVRMDED GYVWVVDRKK DMIISGGENV YCAEVENVLA SHPSIVEVAV IGRADEKWGE VPIAVAAVTK DHLRIEDLDE YLTERLARYK HPKALEIVDA LPRNPSGKVL KTELRLRYGV GVYSESRSVS RSFEFREGS //