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Database: UniProt
Entry: F9Q7Z1_9PAST
LinkDB: F9Q7Z1_9PAST
Original site: F9Q7Z1_9PAST 
ID   F9Q7Z1_9PAST            Unreviewed;       252 AA.
AC   F9Q7Z1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Putative 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:EGV06319.1};
GN   ORFNames=HMPREF9952_1748 {ECO:0000313|EMBL:EGV06319.1};
OS   Haemophilus pittmaniae HK 85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV06319.1, ECO:0000313|Proteomes:UP000006235};
RN   [1] {ECO:0000313|EMBL:EGV06319.1, ECO:0000313|Proteomes:UP000006235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK 85 {ECO:0000313|EMBL:EGV06319.1,
RC   ECO:0000313|Proteomes:UP000006235};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGV06319.1}.
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DR   EMBL; AFUV01000007; EGV06319.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9Q7Z1; -.
DR   STRING; 1035188.HMPREF9952_1748; -.
DR   ESTHER; 9past-f9q7z1; MenH_SHCHC.
DR   UniPathway; UPA00079; -.
DR   UniPathway; UPA01057; UER00900.
DR   Proteomes; UP000006235; Unassembled WGS sequence.
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; PF12697; Abhydrolase_6; 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}.
FT   DOMAIN          6..237
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
SQ   SEQUENCE   252 AA;  28169 MW;  CFB2C1B9915DDA52 CRC64;
     MTTPILILLH GLLGSADDWA PLQRYLTDIP TLALDLPGHG TQRDIAVADF TEASHWLAEK
     IRQHLGEAPY ILLGYSMGGR LALHYVLQSG IPLGDLRGVI VEGANFGLSN AQEKALRWQQ
     DLLWAERFCH ETPQVVLQDW YQQPVFAHLT EEQRQALIRK RSEQCGANIG SILAALSLAK
     QMDFRPLLTQ MPIPFYYFCG AQDNKFQNIS RQAGIEPHLI AAAGHNAHRE NPELFAQKLQ
     NCLLKIADST GK
//
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