MENC_GEOKA
ID MENC_GEOKA Reviewed; 375 AA.
AC Q5L1G9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=o-succinylbenzoate synthase {ECO:0000255|HAMAP-Rule:MF_01933};
DE Short=OSB synthase {ECO:0000255|HAMAP-Rule:MF_01933};
DE Short=OSBS {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000303|PubMed:16584181};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:16584181};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
DE AltName: Full=N-succinylamino acid racemase {ECO:0000303|PubMed:16584181};
DE Short=NSAR {ECO:0000303|PubMed:16584181};
DE EC=5.1.1.- {ECO:0000269|PubMed:16584181};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_01933};
GN OrderedLocusNames=GK0926 {ECO:0000312|EMBL:BAD75211.1};
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=HTA426;
RX PubMed=16584181; DOI=10.1021/bi060230b;
RA Sakai A., Xiang D.F., Xu C., Song L., Yew W.S., Raushel F.M., Gerlt J.A.;
RT "Evolution of enzymatic activities in the enolase superfamily: N-
RT succinylamino acid racemase and a new pathway for the irreversible
RT conversion of D- to L-amino acids.";
RL Biochemistry 45:4455-4462(2006).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:16584181). Also
CC acts as a N-succinylamino acid racemase (NSAR) that catalyzes the
CC racemization of various N-succinylamino acids, including N-succinyl-L-
CC valine, N-succinyl-L-alanine, N-succinyl-L-methionine, N-succinyl-L-
CC tyrosine, N-succinyl-L-serine, N-succinyl-L-isoleucine, N-succinyl-L-
CC phenylalanine and N-succinyl-L-leucine (PubMed:16584181). May be a
CC bifunctional enzyme involved in menaquinone biosynthesis and in an
CC irreversible pathway for the conversion of D- to L-amino acids, thereby
CC facilitating the survival and/or growth of the organism
CC (PubMed:16584181). {ECO:0000269|PubMed:16584181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate
CC = 2-succinylbenzoate + H2O; Xref=Rhea:RHEA:10196, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18325, ChEBI:CHEBI:58689; EC=4.2.1.113;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01933,
CC ECO:0000269|PubMed:16584181};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 mM for N-succinyl-L-valine {ECO:0000269|PubMed:16584181};
CC KM=2.6 mM for N-succinyl-L-alanine {ECO:0000269|PubMed:16584181};
CC KM=3.6 mM for N-succinyl-L-methionine {ECO:0000269|PubMed:16584181};
CC KM=2.6 mM for N-succinyl-L-tyrosine {ECO:0000269|PubMed:16584181};
CC KM=3.0 mM for N-succinyl-L-serine {ECO:0000269|PubMed:16584181};
CC KM=3.7 mM for N-succinyl-L-isoleucine {ECO:0000269|PubMed:16584181};
CC KM=0.8 mM for N-succinyl-L-phenylalanine
CC {ECO:0000269|PubMed:16584181};
CC KM=1.3 mM for N-succinyl-L-leucine {ECO:0000269|PubMed:16584181};
CC Note=kcat is 180 sec(-1) with SHCHC as substrate. kcat is 92 sec(-1)
CC with N-succinyl-L-valine as substrate. kcat is 89 sec(-1) with N-
CC succinyl-L-alanine as substrate. kcat is 53 sec(-1) with N-succinyl-
CC L-methionine as substrate. kcat is 52 sec(-1) with N-succinyl-L-
CC tyrosine as substrate. kcat is 45 sec(-1) with N-succinyl-L-serine as
CC substrate. kcat is 35 sec(-1) with N-succinyl-L-isoleucine as
CC substrate. kcat is 19 sec(-1) with N-succinyl-L-phenylalanine as
CC substrate. kcat is 17 sec(-1) with N-succinyl-L-leucine as substrate.
CC {ECO:0000269|PubMed:16584181};
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
CC {ECO:0000255|HAMAP-Rule:MF_01933}.
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01933}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01933}.
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DR EMBL; BA000043; BAD75211.1; -; Genomic_DNA.
DR RefSeq; WP_011230427.1; NC_006510.1.
DR STRING; 235909.GK0926; -.
DR EnsemblBacteria; BAD75211; BAD75211; GK0926.
DR KEGG; gka:GK0926; -.
DR PATRIC; fig|235909.7.peg.1016; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_4_9; -.
DR OMA; CRIINIK; -.
DR SABIO-RK; Q5L1G9; -.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043748; F:O-succinylbenzoate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03317; NAAAR; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR HAMAP; MF_01933; MenC_2; 1.
DR InterPro; IPR036849; Enolase-like_C_sf.
DR InterPro; IPR029017; Enolase-like_N.
DR InterPro; IPR029065; Enolase_C-like.
DR InterPro; IPR013342; Mandelate_racemase_C.
DR InterPro; IPR013341; Mandelate_racemase_N_dom.
DR InterPro; IPR010197; OSB_synthase_MenC_2.
DR PANTHER; PTHR48073:SF5; PTHR48073:SF5; 1.
DR Pfam; PF13378; MR_MLE_C; 1.
DR Pfam; PF02746; MR_MLE_N; 1.
DR SMART; SM00922; MR_MLE; 1.
DR SUPFAM; SSF51604; SSF51604; 1.
DR SUPFAM; SSF54826; SSF54826; 1.
DR TIGRFAMs; TIGR01928; menC_lowGC/arch; 1.
PE 1: Evidence at protein level;
KW Isomerase; Lyase; Magnesium; Menaquinone biosynthesis; Metal-binding;
KW Reference proteome.
FT CHAIN 1..375
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455098"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01933"
SQ SEQUENCE 375 AA; 41828 MW; 8E5A01E23E3A1585 CRC64;
MAINIEYVIL RHLQMELKAP FTTSFGTFQT KELILVEAVD CDGVSGWGES VAFSAPWYSE
ETVKTNWHML EEFLVPLLFS KPLRHPAELP ERFAAIRQNN MAKAALEGAV WDLYAKRLGV
PLCQALGGTK KEIEVGVSIG IQPTVADLLQ VIERYVAQGY RRIKVKIKPG WDVDVIRDVR
RAFPDVPLMA DANSAYTFAD AKRLQALDEF GLMMIEQPLA ADDLVDHARL QPLLQTPICL
DESIRSYDDA RKALDLGSCR IINIKIGRVG GLWEAKRIHD LCAERGVSVW CGGMLEAGVG
RAHNIAITTL ENFALPGDTA ASSHYWERDI ITPEVEVQGG LIRVPNAPGI GYEVDRRQVE
RYTQFAKVFH RTATA
