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 25-MAY-2022, entry version 86.
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}; 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., Pushparaj V.,
RA Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S.,
RA Shea T., Arachchi H., Macdonald P., Abouelleil A., Lui A., Priest M.,
RA Berlin A., Gearin G., Brown A., Aftuck L., Bessette D., Allen N.,
RA Lubonja R., Lokyitsang T., Matthews C., Dunbar C., Benamara M., Nguyen T.,
RA Negash T., 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 decarboxylation
CC of 2-oxoglutarate and the subsequent addition of the resulting succinic
CC semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-
CC succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
CC {ECO:0000255|HAMAP-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; EC=2.2.1.9;
CC 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. {ECO:0000255|HAMAP-
CC Rule:MF_01659};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
CC {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}.
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DR EMBL; CP000717; ABR04908.1; -; Genomic_DNA.
DR RefSeq; WP_003402927.1; NZ_KK339377.1.
DR AlphaFoldDB; A1QNY1; -.
DR SMR; A1QNY1; -.
DR KEGG; mtf:TBFG_10565; -.
DR PATRIC; fig|336982.11.peg.615; -.
DR HOGENOM; CLU_006051_4_1_11; -.
DR OMA; FCNRGTS; -.
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;
KW Magnesium; Manganese; Menaquinone biosynthesis; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..554
FT /note="2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-
FT carboxylate synthase"
FT /id="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
