(data stored in ACNUC1104 zone)

SWISSPROT: MEND_MYCTF

ID   MEND_MYCTF              Reviewed;         554 AA.
AC   A1QNY1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE            Short=SEPHCHC synthase {ECO:0000255|HAMAP-Rule:MF_01659};
DE            EC=2.2.1.9 {ECO:0000255|HAMAP-Rule:MF_01659};
DE   AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000255|HAMAP-Rule:MF_01659};
GN   Name=menD {ECO:0000255|HAMAP-Rule:MF_01659};
GN   OrderedLocusNames=TBFG_10565;
OS   Mycobacterium tuberculosis (strain F11).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=336982;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11;
RA   Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA   Grabherr M., Mauceli E., Brockman W., Young S., LaButti K.,
RA   Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T.,
RA   Zimmer A., Settipalli S., Shea T., Arachchi H., Macdonald P.,
RA   Abouelleil A., Lui A., Priest M., Berlin A., Gearin G., Brown A.,
RA   Aftuck L., Bessette D., Allen N., Lubonja R., Lokyitsang T.,
RA   Matthews C., Dunbar C., Benamara M., Nguyen T., Negash T.,
RA   DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S.,
RA   Alvarado L., Victor T., Murray M.;
RT   "The complete genome sequence of Mycobacterium tuberculosis F11.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the thiamine diphosphate-dependent
CC       decarboxylation of 2-oxoglutarate and the subsequent addition of
CC       the resulting succinic semialdehyde-thiamine pyrophosphate anion
CC       to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-
CC       cyclohexene-1-carboxylate (SEPHCHC). {ECO:0000255|HAMAP-
CC       Rule:MF_01659}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-
CC         hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2;
CC         Xref=Rhea:RHEA:25593, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29780, ChEBI:CHEBI:58818;
CC         EC=2.2.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01659};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01659};
CC   -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC       biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step
CC       2/7. {ECO:0000255|HAMAP-Rule:MF_01659}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01659}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01659}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01659}.
DR   EMBL; CP000717; ABR04908.1; -; Genomic_DNA.
DR   RefSeq; WP_003402927.1; NZ_KK339377.1.
DR   SMR; A1QNY1; -.
DR   EnsemblBacteria; ABR04908; ABR04908; TBFG_10565.
DR   KEGG; mtf:TBFG_10565; -.
DR   PATRIC; fig|336982.11.peg.615; -.
DR   HOGENOM; HOG000218359; -.
DR   KO; K02551; -.
DR   OMA; AIFDMLP; -.
DR   BioCyc; MTUB336982:G1G92-593-MONOMER; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   GO; GO:0070204; F:2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01659; MenD; 1.
DR   InterPro; IPR004433; MenaQ_synth_MenD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   PANTHER; PTHR42916; PTHR42916; 2.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF004983; MenD; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00173; menD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1QNY1.
DR   SWISS-2DPAGE; A1QNY1.
KW   Magnesium; Manganese; Menaquinone biosynthesis; Metal-binding;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    554       2-succinyl-5-enolpyruvyl-6-hydroxy-3-
FT                                cyclohexene-1-carboxylate synthase.
FT                                /FTId=PRO_0000341786.
SQ   SEQUENCE   554 AA;  57836 MW;  879423AAB00F36A5 CRC64;
     MNPSTTQARV VVDELIRGGV RDVVLCPGSR NAPLAFALQD ADRSGRIRLH VRIDERTAGY
     LAIGLAIGAG APVCVAMTSG TAVANLGPAV VEANYARVPL IVLSANRPYE LLGTGANQTM
     EQLGYFGTQV RASISLGLAE DAPERTSALN ATWRSATCRV LAAATGARTA NAGPVHFDIP
     LREPLVPDPE PLGAVTPPGR PAGKPWTYTP PVTFDQPLDI DLSVDTVVIS GHGAGVHPNL
     AALPTVAEPT APRSGDNPLH PLALPLLRPQ QVIMLGRPTL HRPVSVLLAD AEVPVFALTT
     GPRWPDVSGN SQATGTRAVT TGAPRPAWLD RCAAMNRHAI AAVREQLAAH PLTTGLHVAA
     AVSHALRPGD QLVLGASNPV RDVALAGLDT RGIRVRSNRG VAGIDGTVST AIGAALAYEG
     AHERTGSPDS PPRTIALIGD LTFVHDSSGL LIGPTEPIPR SLTIVVSNDN GGGIFELLEQ
     GDPRFSDVSS RIFGTPHDVD VGALCRAYHV ESRQIEVDEL GPTLDQPGAG MRVLEVKADR
     SSLRQLHAAI KAAL
//

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