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Database: UniProt
Entry: A0A087SN26_AUXPR
LinkDB: A0A087SN26_AUXPR
Original site: A0A087SN26_AUXPR 
ID   A0A087SN26_AUXPR        Unreviewed;      1048 AA.
AC   A0A087SN26;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=isochorismate synthase {ECO:0000256|ARBA:ARBA00012824};
DE            EC=5.4.4.2 {ECO:0000256|ARBA:ARBA00012824};
GN   ORFNames=F751_1303 {ECO:0000313|EMBL:KFM27130.1};
OS   Auxenochlorella protothecoides (Green microalga) (Chlorella
OS   protothecoides).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Auxenochlorella.
OX   NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM27130.1, ECO:0000313|Proteomes:UP000028924};
RN   [1] {ECO:0000313|EMBL:KFM27130.1, ECO:0000313|Proteomes:UP000028924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0710 {ECO:0000313|EMBL:KFM27130.1,
RC   ECO:0000313|Proteomes:UP000028924};
RX   PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA   Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT   "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT   protothecoides revealed through its genome, transcriptomes, and
RT   proteomes.";
RL   BMC Genomics 15:582-582(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC         ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000799};
CC   -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC       {ECO:0000256|ARBA:ARBA00005297}.
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DR   EMBL; KL662143; KFM27130.1; -; Genomic_DNA.
DR   RefSeq; XP_011400097.1; XM_011401795.1.
DR   AlphaFoldDB; A0A087SN26; -.
DR   STRING; 3075.A0A087SN26; -.
DR   GeneID; 23612694; -.
DR   KEGG; apro:F751_1303; -.
DR   eggNOG; KOG1223; Eukaryota.
DR   OrthoDB; 298598at2759; -.
DR   Proteomes; UP000028924; Unassembled WGS sequence.
DR   GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:InterPro.
DR   GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:InterPro.
DR   CDD; cd07037; TPP_PYR_MenD; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   HAMAP; MF_01659; MenD; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Chorismate_C.
DR   InterPro; IPR004561; IsoChor_synthase.
DR   InterPro; IPR004433; MenaQ_synth_MenD.
DR   InterPro; IPR032264; MenD_middle.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   NCBIfam; TIGR00543; isochor_syn; 1.
DR   NCBIfam; TIGR00173; menD; 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; PF00425; Chorismate_bind; 1.
DR   Pfam; PF16582; TPP_enzyme_M_2; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT   DOMAIN          258..511
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   DOMAIN          545..656
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          719..959
FT                   /note="Menaquinone biosynthesis protein MenD middle"
FT                   /evidence="ECO:0000259|Pfam:PF16582"
SQ   SEQUENCE   1048 AA;  108722 MW;  A773FAE41C791421 CRC64;
     MPAPSPPPPP VHVHCQTLPP CKDLAAGKEQ VEKALDAAVA ARAGLPAALI RCEAQVPRTH
     SALAWLQAQR AGTSGAAAPS RPAPTLYFSP RLSPGPDSAG AAAAACEEGA GAVAGVGAAA
     LWRGAPGEAL DAARLHGMQR FTSAAAPRVR ALGGSRFDAQ RGLSPEWAAF GTFTFLIPSV
     EAAVTLAQEL LDEESAEGEA APCTPSLLDP GTALENYIAG GQQGLDDLLE ALEGTPALGA
     PATGGDCGTR DPDCGAAALS KVVLARRSEL RLSGGADPLA LLASLQARNP RAYALFLELE
     GGEAFLSCTP ERLYSRSGRS VASEAVAGTR ARGGGSVEND FWLALDLLQS KKEHAEFTIV
     RDWVYEALRG ICATVRVDVR KTVLKQESLQ HLYGQLSGTL LPAATDADLL AALHPTPAVC
     GRPREASRDM LSSLEPFDRG FYSGPFGWLG GQGAEFAVAI RSALFVPEVQ APEFPGVQAL
     GPTAMRVALY AGVGIVPGSK ASLEWAELDL KVAALDRLLT PVPALQQARK RGSQWGAPNL
     NAAYARILVE ELCRLGCSTF CIAPGSRSSP LTLAAAQHPR VQLVSGMDER SLAFWALGHG
     RSGAAPAVIL TTSGTAVANL LPAAVEGWQS GTPLIILTAD RPAEVRGSGA NQTIHQPGIF
     SSYVCWQADL APPSSAMPPQ HLLGSLDRAV AAAGAGPVHL NVQLREPLGP VPEPWESTAW
     LEGLGDWATS SRPWSVQLEA AACASRLPHS LLAALSTATR GLLVAGELRA PEDRAAALAV
     SRALRWPLLA DVLSGLRVGA TGVPEGLIAC GDNILAAQDP GMCTALRPDV VLQLGGRLTS
     KRISAFLAAS SARGSSAGND SAAWWVVDAS PHSFDEHGCL AGRVRLPLGA LERLLREAGV
     LVEGAAAAPF TSPYLELWRT MDREVGFLVR QRLNSAPYGE AHIAACLASS LPRGHALYIG
     NSMPIRDMDM FADGLALSGC TQGQVPSLGC PVGANRGASG IDGVLSSAAG FASGLGMPTT
     LVVGDLSFLH DTNGLMLLRS GKETWDRA
//
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