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Database: UniProt
Entry: A0A0L6WPK1_9AGAR
LinkDB: A0A0L6WPK1_9AGAR
Original site: A0A0L6WPK1_9AGAR 
ID   A0A0L6WPK1_9AGAR        Unreviewed;       583 AA.
AC   A0A0L6WPK1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=2-succinylbenzoate--CoA ligase {ECO:0000313|EMBL:KNZ77059.1};
GN   ORFNames=J132_07453 {ECO:0000313|EMBL:KNZ77059.1};
OS   Termitomyces sp. J132.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Termitomyces.
OX   NCBI_TaxID=1306850 {ECO:0000313|EMBL:KNZ77059.1, ECO:0000313|Proteomes:UP000053712};
RN   [1] {ECO:0000313|Proteomes:UP000053712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J132 {ECO:0000313|Proteomes:UP000053712};
RA   Hu H., Poulsen M.;
RT   "The genome of Termitomyces.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ412544; KNZ77059.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6WPK1; -.
DR   STRING; 1306850.A0A0L6WPK1; -.
DR   OrthoDB; 2433631at2759; -.
DR   Proteomes; UP000053712; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:KNZ77059.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053712};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        113..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          57..413
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          467..544
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   583 AA;  64240 MW;  E854B99F39ABAF19 CRC64;
     MADAIKKPWY AQRTLAETDA IITAPGSPFE LETRYIDGRL QRVYKRLYPS LRTFWLWAAA
     EHADLTYVVL ENQRISYKQA FQQSLRAAGV LRDVYGVKKG DRVGICSRNY PDYVVAFWAC
     HLIGAVSVLV NAWLPQNQLL FCLVHTECKV IILDPERADR LEASVEELKK AAKSNGILVF
     NSHEGKGKWN GMKSWNAVLA AYNGDIKGIE TGRGEEGILP EDNAAILFTS GTTGMPKGVL
     STQRQFLTNL FNTLRPTTDS INLPLMIATF SGHKVILMRR WIPEEGARLI KEESCTIAGG
     VPSMVMDLLE TSLADSGYPL ESFSFGGAPA PDVLTEKATK LFPTAVLGQG YGMTETNSLA
     VGISGEDCIA RPQSTGLPTP VNELVIVKGD MAMPPGELGE VWIRGVNVMK GYWRDPEATE
     KASAVTKDGW MKTGDLGYLD EEGYLYVKDR IKDIIIRGGE NIDSTTVENA LYADSRVMEA
     AAVAVPHERL GEVVAAVVAV KPAFKGQVTE ASLIAIATKS LPKFAVPVMV IVRDELLEKN
     ASGKIVKMPL RRMAREIWQK RQSELKTKLQ ELSARDRSRV EDV
//
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