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
//