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Database: UniProt
Entry: C9ZEH2_STRSW
LinkDB: C9ZEH2_STRSW
Original site: C9ZEH2_STRSW 
ID   C9ZEH2_STRSW            Unreviewed;       530 AA.
AC   C9ZEH2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Putative substrate-CoA ligase {ECO:0000313|EMBL:CBG67431.1};
GN   OrderedLocusNames=SCAB_2131 {ECO:0000313|EMBL:CBG67431.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG67431.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG67431.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG67431.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
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DR   EMBL; FN554889; CBG67431.1; -; Genomic_DNA.
DR   RefSeq; WP_012998168.1; NC_013929.1.
DR   AlphaFoldDB; C9ZEH2; -.
DR   STRING; 680198.SCAB_2131; -.
DR   GeneID; 24306283; -.
DR   KEGG; scb:SCAB_2131; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_0_11; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; IPR020459; AMP-binding.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:CBG67431.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT   DOMAIN          15..380
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          431..506
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   530 AA;  57168 MW;  8AA8461D29EE0B6F CRC64;
     MAAVDISPAT ALHRRAQHPG PPAVVYENRE ITAVELGATV GEFAAGLSEH GLRRGDRIAY
     LGLNSVTFLE TLFAAARLGA VFVPLNFRLA ADEVRHILND CGAHTVVVEE GHRELVESIL
     HDIPARTRLL VDTDPACPAT GTPAPAWTPL STLRGPHRPV REPVALYDDD LAALMYTSGT
     TGRPKGVMLT HGNLWWNAVN VDAVVDTRAD DVNLALAPLF HIGGLNAFTL RTLVRGGTVV
     LRRSFEPAQC LRDLVEHRVN TFFAVPAMYA ALARVPGFAD ADLGALRSAI VAGAPVPPQL
     IRDYGEVGLS LQQAWGLTET APFATYLPAR LLPEKAGSAG VAMPYTEIRL THPGTGTGIE
     EPDTRGEICV RGPNVTSGYW DNPDATRGAF DDMGWFHTGD IAYRDKDGFY HIVDRLKDMI
     ISGGENVYPA EVERVLAELP GVLEAAVVGV PDARWGETVL AVLSCAAGAE PTVEEVRAFA
     DRYLARYKLP TDVLVIDRLP RNASGKLDKI ELRRWVTARR NAPSTATATA
//
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