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Database: UniProt
Entry: H2IPR3_RAHAC
LinkDB: H2IPR3_RAHAC
Original site: H2IPR3_RAHAC 
ID   H2IPR3_RAHAC            Unreviewed;       557 AA.
AC   H2IPR3;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01659};
DE            Short=SEPHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01659};
DE            EC=2.2.1.9 {ECO:0000256|HAMAP-Rule:MF_01659};
DE   AltName: Full=Menaquinone biosynthesis protein MenD {ECO:0000256|HAMAP-Rule:MF_01659};
GN   Name=menD {ECO:0000256|HAMAP-Rule:MF_01659};
GN   OrderedLocusNames=Rahaq2_1350 {ECO:0000313|EMBL:AEX51230.1};
OS   Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS   NCIMB 13365 / CIP 78.65).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX51230.1, ECO:0000313|Proteomes:UP000009010};
RN   [1] {ECO:0000313|EMBL:AEX51230.1, ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX   PubMed=22582378; DOI=10.1128/JB.00380-12;
RA   Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA   Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA   Tapia R., Woyke T., Sobecky P.A.;
RT   "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL   J. Bacteriol. 194:3020-3021(2012).
RN   [2] {ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA   Martinez R., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL   Submitted (JAN-2012) 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:0000256|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:0000256|HAMAP-Rule:MF_01659};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01659};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01659}.
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01659}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01659}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. MenD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01659}.
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DR   EMBL; CP003244; AEX51230.1; -; Genomic_DNA.
DR   RefSeq; WP_015696472.1; NC_016818.1.
DR   AlphaFoldDB; H2IPR3; -.
DR   STRING; 745277.Rahaq2_1350; -.
DR   GeneID; 61511451; -.
DR   KEGG; raq:Rahaq2_1350; -.
DR   PATRIC; fig|745277.3.peg.1286; -.
DR   eggNOG; COG1165; Bacteria.
DR   HOGENOM; CLU_006051_3_0_6; -.
DR   OMA; FCNRGTS; -.
DR   OrthoDB; 9791859at2; -.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00164.
DR   Proteomes; UP000009010; Chromosome.
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   CDD; cd07037; TPP_PYR_MenD; 1.
DR   CDD; cd02009; TPP_SHCHC_synthase; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   HAMAP; MF_01659; MenD; 1.
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   InterPro; IPR011766; TPP_enzyme_TPP-bd.
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; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF16582; TPP_enzyme_M_2; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF004983; MenD; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01659};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01659};
KW   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01659};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01659}; Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW   Thiamine pyrophosphate {ECO:0000256|HAMAP-Rule:MF_01659};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01659}.
FT   DOMAIN          11..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          183..389
FT                   /note="Menaquinone biosynthesis protein MenD middle"
FT                   /evidence="ECO:0000259|Pfam:PF16582"
FT   DOMAIN          413..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   557 AA;  60520 MW;  17639C961B955501 CRC64;
     MSVAVFNRRW ATLILEALTR HQVQHVCIAP GSRSTPLTLA AAAHPHLICH THFDERGLGH
     LALGLAKASG KRVAIIVTSG TAVANLYPAL IEAGLTGEKL VLLTADRPPE LINCGANQAI
     RQTGMFASHP VGTLDLPRPT PEISARWLVS ALDNALAQQT HGAVHINCPF AEPLYGEDNG
     EHQDWLQTLG DWWQGHQPWL SYSQVLPATA QPDWFSWRQK RGVIIAGRLS ACESEQVAQW
     AAQLGWPLIS DVQASTGNPL PCADLWLASP QAQAILAHVQ LVIQFGGGLT GKRLLQWQAT
     CQPDEYWLVD PLSGRQDPAQ HRGRRLQASV SEWLQSHPAQ SQPDWAESLE HCSQRALHAV
     ETRLEGVFGE AATAWQLPAL LPEHGQLFLG NSLIVRLVDA FAQLPTGYSV FANRGASGID
     GLLSTAAGVQ RATCKPTLVL LGDISALYDL NALALMRQCS APTVIIVVNN NGGQIFSLLP
     TPEAERQRFY CMPQNVSFSH AAAMFGLDYA CPTSMSELHH AVRQCWQHGG VKLIELKVSE
     TEGAECLRSL VQEMSAS
//
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