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Database: UniProt
Entry: D9W4P7_9ACTN
LinkDB: D9W4P7_9ACTN
Original site: D9W4P7_9ACTN 
ID   D9W4P7_9ACTN            Unreviewed;       580 AA.
AC   D9W4P7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=O-succinylbenzoate-CoA ligase {ECO:0000313|EMBL:EFL19875.1};
GN   ORFNames=SSNG_07127 {ECO:0000313|EMBL:EFL19875.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL19875.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL19875.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL19875.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657751; EFL19875.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9W4P7; -.
DR   STRING; 253839.SSNG_07127; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_11; -.
DR   Proteomes; UP000005763; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR036736; ACP-like_sf.
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   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR43352; ACETYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43352:SF1; P-HYDROXYBENZOIC ACID--AMP LIGASE FADD22; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EFL19875.1}.
FT   DOMAIN          2..59
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|Pfam:PF00550"
FT   DOMAIN          83..439
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          490..567
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   580 AA;  59796 MW;  51654E2907643ADB CRC64;
     MASVLQVDKD AIEPGAQFYE ELGMSSLEKT EVVVAVEREF GALSAQEAAA FTSLDAAVAV
     LGERATSLQG IDLIDRLVVR HVSAGRGDRA SYLDPQAGEI TYAGLLEAAR GYAGALRTAG
     VPEGARGLLV ADDSVATVAA VLGLWWHGCI PVVISPVLTD DEVRYIAADC SAAMVHLDAA
     PARQRALEEL FTTTTRFAGA DVRAGLATAS AGPAYHPEVA GPPAAWRAVG EALVQYTSGS
     TGMPKGVRHS AGAIAAMADG VGTVLALTPD DTVLSSARMS FGYGFGSSVL CPLAAGARVA
     LISGTVDVHS LTAALQHHRP TVLFSVPRLY AALLNTSGTK LSPESVDSVR LCVAAGENLP
     GPLSERIRAA FQAELLNGLG ATEVLYIVVG TPPKEDRPGT FGVPVPGITA TVRAADGTPV
     AEGKQGRLHI AGPTVALGYI GRPEAAAVTF ADGGAYTGDV VHREPDGTFT HLCRADDVLN
     LGGYKVVPSE IESVVRGVDG VQDCVVVGSR DADGLEQAVA YLVARPGSDK AVVRRAVTAA
     IRGGLAAFKR PARLEFLDQL PTTSTGKVAA FELRKAAARP
//
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