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Database: UniProt
Entry: A0A0A2W5D7_BEABA
LinkDB: A0A0A2W5D7_BEABA
Original site: A0A0A2W5D7_BEABA 
ID   A0A0A2W5D7_BEABA        Unreviewed;      2548 AA.
AC   A0A0A2W5D7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000313|EMBL:KGQ13902.1};
GN   ORFNames=BBAD15_g150 {ECO:0000313|EMBL:KGQ13902.1};
OS   Beauveria bassiana D1-5.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ13902.1, ECO:0000313|Proteomes:UP000030106};
RN   [1] {ECO:0000313|EMBL:KGQ13902.1, ECO:0000313|Proteomes:UP000030106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1-5 {ECO:0000313|EMBL:KGQ13902.1,
RC   ECO:0000313|Proteomes:UP000030106};
RA   Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA   Du Q., Sun Z.;
RT   "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT   bassiana D1-5.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA +
CC         H2O; Xref=Rhea:RHEA:26562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57364, ChEBI:CHEBI:58897; EC=4.1.3.36;
CC         Evidence={ECO:0000256|ARBA:ARBA00000177};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ13902.1}.
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DR   EMBL; ANFO01000014; KGQ13902.1; -; Genomic_DNA.
DR   STRING; 1245745.A0A0A2W5D7; -.
DR   HOGENOM; CLU_228194_0_0_1; -.
DR   Proteomes; UP000030106; Unassembled WGS sequence.
DR   GO; GO:0008935; F:1,4-dihydroxy-2-naphthoyl-CoA synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:InterPro.
DR   GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd06558; crotonase-like; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   CDD; cd17630; OSB_MenE-like; 1.
DR   CDD; cd03320; OSBS; 1.
DR   CDD; cd07037; TPP_PYR_MenD; 1.
DR   CDD; cd02009; TPP_SHCHC_synthase; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR   HAMAP; MF_01934; MenB; 1.
DR   HAMAP; MF_00470; MenC_1; 1.
DR   HAMAP; MF_01659; MenD; 1.
DR   HAMAP; MF_01660; MenH; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR005801; ADC_synthase.
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; IPR015890; Chorismate_C.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR010198; DHNA-CoA_synthase_MenB.
DR   InterPro; IPR043605; DUF883_C.
DR   InterPro; IPR043604; DUF883_N.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR004433; MenaQ_synth_MenD.
DR   InterPro; IPR048639; MenC_N.
DR   InterPro; IPR032264; MenD_middle.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-like.
DR   InterPro; IPR010196; OSB_synthase_MenC1.
DR   InterPro; IPR022485; SHCHC_synthase_MenH.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR01929; menB; 1.
DR   NCBIfam; TIGR01927; menC_gam_Gplu; 1.
DR   NCBIfam; TIGR00173; menD; 1.
DR   NCBIfam; TIGR03695; menH_SHCHC; 1.
DR   PANTHER; PTHR42916; 2-SUCCINYL-5-ENOLPYRUVYL-6-HYDROXY-3-CYCLOHEXENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR42916:SF1; PROTEIN PHYLLO, CHLOROPLASTIC; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   Pfam; PF13673; Acetyltransf_10; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF05957; DUF883; 1.
DR   Pfam; PF19029; DUF883_C; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   Pfam; PF21508; MenC_N; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF05368; NmrA; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF16582; TPP_enzyme_M_2; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
DR   SFLD; SFLDF00009; o-succinylbenzoate_synthase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          250..396
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   2548 AA;  279164 MW;  5DB889CA30A95BA8 CRC64;
     MFAITGITGQ VGGALAEALL AQGHEIRAVV RSETKGQLWA QQGADIALAE MHDGEALAQA
     FSGAEAVFIL LPPVFDPSGN MAEPRAHIAA IRHALLAARP RHVVCLSTIG AQATQPNLLN
     ALGLMEKELT DVCHSVVFLR AGWFMENFLW DVESAKETGT VYSHLQPLAR AIPMIATVDI
     GLLAAELLTQ PESGTRIVEL EGPQRYSPHL AAEAFSQVLG RPVTVKAVPR ENWEADFLAQ
     GMKNPLPRMK MLDGFNEGWI DFTGETVKAL RCEVFIVEQR CAYLDVDGED LVGENRHILG
     WRDGKLIAYA RILKSDNELE PVVIGRVIVD ASVRGEKLGQ QLMTQALAAC QRQWPERAIY
     LGAQAHLQAF YAQFGFHPVT EVYDEDVMQP YESRLDDDLA LLSDTLEEVL RASGDPADQK
     YIELKEKAEQ ALNDVKARIS NASDNYYYRT KKAVYRADDY VHEKPWQGIG IGAAQMQQEL
     AGEFADEPGL QRLCVPVTLS DASDPLAWLT AQSRYPQFYW QQRNGNEEVA ALGALLSFSA
     LEDAQAFLQS HPEQPFLRVW GLNAFDPSHG FLFLSRLEWR RDAIAAAAFI EQLLPAKLLP
     QLNLKCLGET HLPEQPEWHR LVDQVVSAIS QNALDKVVLA RATDLAFSSP VSAAGFMAAS
     RRVNLNCYHF LMAFDEKNAF LGSSPERLWR RIDDALRTEA LAGTVANHPD DAQAAKLGQW
     LLKDDKNQRE NMLVVEDICQ RLQAAVGALD VLPPQVMRLR KVQHLRRCIW TQLKRQDDAL
     CLKQLQPTAA VAGLPRELAR EFIAANEPFE RECSFNRRWA GVILEALTRH GVRHVCIAPG
     SRSTPLTLSA ADNRSFICHT HFDERGLGHL ALGLAKASGE PVAIIVTSGT AVANLYPAVI
     EAGLTGEKLI LLTADRPPEL IDCGANQAIR QPGLFSSHPS AELNLPRPTH DIPASWLVSA
     IDSAVGQLHG GALHINCPFA EPLYGAPDDT GVDWQNQLGD WWEGNAPWLR EGHENAVPKQ
     RDWFFWRQKR GVVVAGRLSA SAGEQVAAWA QMLGWPLIGD VLSQTGQPLP CADLWLSNSQ
     AVTCLEQAQI VIQFGGSLTG KRVLQWQAAC RPEEYWLVDS QPGRLDPANH RGRRLVARVE
     DWLEKHPAEK RLPWAETLTS LAWQTLEKVE QGTSEFGEAQ VAQRLPQLLP EGGQLFVGNS
     LIVRLIDAFA QLPVGYPVYS NRGASGIDGL LSTAAGVQRA TARSTLAIVG DISALYDLNA
     LALLRHASAP FVLLVVNNNG GQIFSLLPTP AEERERFYCM PQNVNFSHAA AMFELGYQNP
     DSWPALDEAV RRAWLRPGAT VIEITVPETA GAQTLQHLLA QLSVDLPGHG GSADVPVRDF
     ADVEGALRNT LKHHGINDYW LVGYSLGGRI AMYHASRPDV QGLRGLVVEG SHPGLVSEAE
     REARALNDAR WAQRLMHENF QAVLNAWYQQ PVFRSLSPEQ RADLVAFRAK NTPKALAGML
     EATSLARQPN LREPLGQLAA PFHFICGERD AKFRSVAAEL SCSLTLISGA GHNAHREAPA
     AFSSALLTLF RHYDLDGIAK ITINRPEVRN AFRPLTVKEM INALADARYD DNIGTIILTG
     EGEKAFCAGG DQKVRGDYGG YQDASGVHHL NVLDFQRQIR TCPKPVVAMV AGFSIGGGHV
     LHMMCDLTIA AENAVFGQTG PKVGSFDGGW GASYMARIVG QKKAREIWFL CRQYDAKEAL
     DMGLVNTVVP IADLEKETVR WCREMLQNSP MALRCLKAAL NADCDGQAGL QELAGNATML
     FYMTEEGQEG RNAAALWRFQ IPMEAGVVLR DQRLKFREGL LVRLTLGDSS GWGEISPLPG
     FSRESLAEAQ GQAERWLEQW VADESAPLPD LPSVAFGLSC ALAEAEGRLP QAADYRVAPL
     CTGDPDELIL ALAKMSGDKT AKVKVGLYEA VRDGMVVNLL LEAVPELRLR LDANRSWTPL
     KAQQFAKYVN PAHRSRIDFI EEPCKTREQS REFSRETGIA IAWDESLREV DFTFSAEPGV
     AALVIKPTLT GSLEKVREQV AAAHKLGLKA VISSSIESSL GLTQLARIAA WLTPGTLPGL
     DTLSLMQSQA RAYSMIFTDW PWRHWANVRG AGVALRLDDD LLTWETLCQR VDALAGGFRQ
     QGVKEGDGVA LKAKNGPQTL LVWLALWQCG ARILPLNPQL PDSLLAQLLP SLTLSYGITL
     PGDEPFPDVA PLSLVSAPAW CEAWLPSRFA SMTLTSGSTG LPKAAVHTCS AHLASAAGVL
     AMMNYGADDS WLLSLPLFHV SGQGILWRWL YAGGHHASLV PTQLWRLLEK QEPLALREVL
     LGGAAIPVEL TQQAEARGVR CWCGYGLTEL ASTVCAKRAD GQPDVGAPLP GRKVKIVDEE
     VWIQADSLAS GYWRDGCLIP LGNEQGWFAT RDRGVLRAGR LTIVGRLDNQ FFSGGEGIQP
     EEVERVIAAH PAVQQVFVVP VDDAEFGQRP VAVVEISAGC EVNDIAAWLD GKLPRFQRPV
     RWLPLPQALK QGGIKISRRT LIAWAAGA
//
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