ID D8MUS5_ERWBE Unreviewed; 257 AA.
AC D8MUS5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase {ECO:0000256|HAMAP-Rule:MF_01660};
DE Short=SHCHC synthase {ECO:0000256|HAMAP-Rule:MF_01660};
DE EC=4.2.99.20 {ECO:0000256|HAMAP-Rule:MF_01660};
GN Name=menH {ECO:0000256|HAMAP-Rule:MF_01660,
GN ECO:0000313|EMBL:CAX60582.1};
GN OrderedLocusNames=EbC_30510 {ECO:0000313|EMBL:CAX60582.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|EMBL:CAX60582.1, ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX60582.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX60582.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
CC -!- FUNCTION: Catalyzes a proton abstraction reaction that results in 2,5-
CC elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-
CC cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-
CC hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). {ECO:0000256|HAMAP-
CC Rule:MF_01660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-
CC carboxylate = (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-
CC carboxylate + pyruvate; Xref=Rhea:RHEA:25597, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:58689, ChEBI:CHEBI:58818; EC=4.2.99.20;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01660};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 3/7.
CC {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01660}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family.
CC {ECO:0000256|HAMAP-Rule:MF_01660}.
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DR EMBL; FP236843; CAX60582.1; -; Genomic_DNA.
DR RefSeq; WP_013203067.1; NC_014306.1.
DR AlphaFoldDB; D8MUS5; -.
DR STRING; 634500.EbC_30510; -.
DR ESTHER; erwbe-d8mus5; MenH_SHCHC.
DR MEROPS; S33.996; -.
DR KEGG; ebi:EbC_30510; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_38_2_6; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00900.
DR Proteomes; UP000008793; Chromosome.
DR GO; GO:0070205; F:2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR HAMAP; MF_01660; MenH; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR022485; SHCHC_synthase_MenH.
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; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01660};
KW Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428, ECO:0000256|HAMAP-
KW Rule:MF_01660}; Reference proteome {ECO:0000313|Proteomes:UP000008793}.
FT DOMAIN 16..239
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 257 AA; 28512 MW; 3E72CDA61A1A16D9 CRC64;
MILHACWQGK RRPDRPVLVW LHGLLGSARD WQPVQSLLAD WPQLAIDLPG HGGSQAHPVG
GFEPLSENIN QTLRRYHVGR YWLIGYSLGG RVALYHACRH AGSALQGLVV EGAHFGLNDP
AQRQQRQAQD ARWAEDFRTL PLAQTLDAWY RQPIFAGLTG QQRAALIAAR SGNHPAAIAA
MLQATSLSQQ PCLLAELRHL QRPFSYFCGE HDQKFRQLAQ QASLPCTPIP AAGHNAHREN
PVAFAGLLAQ RLHSEEH
//
