ID B2W1Q7_PYRTR Unreviewed; 514 AA.
AC B2W1Q7;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=2-succinylbenzoate-CoA ligase {ECO:0000313|EMBL:EDU47230.1};
GN ORFNames=PTRG_04392 {ECO:0000313|EMBL:EDU47230.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU47230.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; DS231617; EDU47230.1; -; Genomic_DNA.
DR RefSeq; XP_001934725.1; XM_001934690.1.
DR AlphaFoldDB; B2W1Q7; -.
DR STRING; 426418.B2W1Q7; -.
DR EnsemblFungi; EDU47230; EDU47230; PTRG_04392.
DR GeneID; 6342630; -.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_0_1; -.
DR InParanoid; B2W1Q7; -.
DR OMA; FRGYYRS; -.
DR OrthoDB; 3109088at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05926; FACL_fum10p_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 InterPro; IPR045310; Pcs60-like.
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 SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EDU47230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 12..368
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 419..494
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 514 AA; 55482 MW; ADAC9BBE0138329A CRC64;
MSPTTLEHAF SKDSSSTAII VPGSPALTVS YKKLAVDVKS FQQKLAKVGV SAEAAVSIAL
PNTYEFIVSF IAASWQRAIA APLNPAYKQS EFEFYIDDLS SAIALVPKGA FAQDAAAVRA
ARKYNAAIAE CYYNGSEVVL DVKETGKLAG KSAPVLSAQP DDVALVLHTS GTTGRPKAVP
LTHRNLLRTM KNIQGTYELT AKDRTMLVMP LFHVHGLLAG FLAPLASGGS VVVPPKFSAS
VFWKDFNEHK ANWYTAVPTI HQILLRSPLP SPMPKIRFIR SCSSPLSPKT FYELEKAFGA
PVLEAYAMTE AAHQMTSNPL PPHQRKPGSV GVGQGVEVKI LDEAGNEVAQ GKEAEICIKG
ENVTNGYLNN PAANASSFTK DGFFRTGDQG KVDSEGYVII TGRIKELINK GGEKISPIEL
DNVIAQHPAV SEAVSFAIED EMYGQDVGLA VVIKEGQALT TGELKTWLTD HVAKFKLPKQ
IFFTDIMPKT ATGKIQRRLV AEAMLKQEQP KAKL
//
