MENC_GEOSE
ID MENC_GEOSE Reviewed; 375 AA.
AC A0A0P0ZBS7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 25.
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};
DE EC=4.2.1.113 {ECO:0000255|HAMAP-Rule:MF_01933};
DE AltName: Full=4-(2'-carboxyphenyl)-4-oxybutyric acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
DE AltName: Full=N-acylamino acid racemase {ECO:0000305};
DE Short=NAAAR {ECO:0000305};
DE AltName: Full=N-succinylamino acid racemase {ECO:0000303|PubMed:25875730};
DE Short=NSAAR {ECO:0000303|PubMed:25875730};
DE Short=NSAR {ECO:0000305};
DE EC=5.1.1.- {ECO:0000269|PubMed:25875730};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_01933};
GN Synonyms=NSAR {ECO:0000312|EMBL:BAT31602.1};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RA Sumida Y., Iwai S., Nishiya Y., Kumagai S., Yamada H., Azuma M.;
RT "Identification and characterization of D-succinylase, and a proposed
RT enzymatic method for D-amino acid synthesis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, AND MUTAGENESIS OF LYS-166; ASP-191; GLU-216; ASP-241 AND LYS-265.
RC STRAIN=CECT49;
RX PubMed=25875730; DOI=10.1007/s12033-015-9839-4;
RA Soriano-Maldonado P., Andujar-Sanchez M., Clemente-Jimenez J.M.,
RA Rodriguez-Vico F., Las Heras-Vazquez F.J., Martinez-Rodriguez S.;
RT "Biochemical and mutational characterization of N-succinyl-amino acid
RT racemase from Geobacillus stearothermophilus CECT49.";
RL Mol. Biotechnol. 57:454-465(2015).
CC -!- FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-
CC carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (By similarity). Also
CC acts as a N-succinylamino acid racemase (NSAR) that catalyzes the
CC racemization of N-succinyl-D/L-phenylalanine (PubMed:25875730). Can
CC catalyze the racemization of a broad range of N-acylamino acids,
CC including N-acetyl-D-methionine, N-formyl-D/L-methionine, N-formyl-D/L-
CC norleucine, N-formyl-D/L-aminobutyric acid, N-formyl-D/L-norvaline, N-
CC formyl-D/L-homophenylalanine, N-carbamoyl-D-methionine and N-carbamoyl-
CC D-norleucine (PubMed:25875730). May be a bifunctional enzyme involved
CC in menaquinone biosynthesis and in an irreversible pathway for the
CC conversion of D- to L-amino acids, thereby facilitating the survival
CC and/or growth of the organism (By similarity).
CC {ECO:0000250|UniProtKB:Q5L1G9, ECO:0000255|HAMAP-Rule:MF_01933,
CC ECO:0000269|PubMed:25875730}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=N(alpha)-acetyl-D-methionine = N(alpha)-acetyl-L-methionine;
CC Xref=Rhea:RHEA:59960, ChEBI:CHEBI:71670, ChEBI:CHEBI:85220;
CC Evidence={ECO:0000269|PubMed:25875730};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01933,
CC ECO:0000269|PubMed:25875730};
CC Note=Shows highest activity in vitro with Co(2+) and Ni(2+).
CC {ECO:0000269|PubMed:25875730};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.6 mM for N-formyl-D-methionine {ECO:0000269|PubMed:25875730};
CC KM=9.0 mM for N-formyl-L-methionine {ECO:0000269|PubMed:25875730};
CC KM=11.1 mM for N-formyl-D-norleucine {ECO:0000269|PubMed:25875730};
CC KM=12.5 mM for N-formyl-L-norleucine {ECO:0000269|PubMed:25875730};
CC KM=19.6 mM for N-formyl-D-aminobutyric acid
CC {ECO:0000269|PubMed:25875730};
CC KM=17.9 mM for N-formyl-L-aminobutyric acid
CC {ECO:0000269|PubMed:25875730};
CC KM=9.2 mM for N-formyl-D-norvaline {ECO:0000269|PubMed:25875730};
CC KM=24.5 mM for N-formyl-L-norvaline {ECO:0000269|PubMed:25875730};
CC KM=3.0 mM for N-formyl-D-homophenylalanine
CC {ECO:0000269|PubMed:25875730};
CC KM=5.7 mM for N-formyl-L-homophenylalanine
CC {ECO:0000269|PubMed:25875730};
CC Note=kcat is 74.6 sec(-1) with N-formyl-D-methionine as substrate.
CC kcat is 52.9 sec(-1) with N-formyl-L-methionine as substrate. kcat is
CC 12.3 sec(-1) with N-formyl-D-norleucine as substrate. kcat is 8.0
CC sec(-1) with N-formyl-L-norleucine as substrate. kcat is 15.2 sec(-1)
CC with N-formyl-D-aminobutyric acid as substrate. kcat is 11.6 sec(-1)
CC with N-formyl-L-aminobutyric acid as substrate. kcat is 11.2 sec(-1)
CC with N-formyl-D-norvaline as substrate. kcat is 19.6 sec(-1) with N-
CC formyl-L-norvaline as substrate. kcat is 88.4 sec(-1) with N-formyl-
CC D-homophenylalanine as substrate. kcat is 85.5 sec(-1) with N-formyl-
CC L-homophenylalanine as substrate. {ECO:0000269|PubMed:25875730};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:25875730};
CC Temperature dependence:
CC Optimum temperature is 55-65 degrees Celsius.
CC {ECO:0000269|PubMed:25875730};
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:25875730}.
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; LC090555; BAT31602.1; -; Genomic_DNA.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA01057; UER00165.
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.
FT CHAIN 1..375
FT /note="o-succinylbenzoate synthase"
FT /id="PRO_0000455099"
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"
FT MUTAGEN 166
FT /note="K->A: Almost loss of activity with N-formyl-D/L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:25875730"
FT MUTAGEN 191
FT /note="D->A: Almost loss of activity with N-formyl-D/L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:25875730"
FT MUTAGEN 216
FT /note="E->A: Almost loss of activity with N-formyl-D/L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:25875730"
FT MUTAGEN 241
FT /note="D->A: Almost loss of activity with N-formyl-D/L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:25875730"
FT MUTAGEN 265
FT /note="K->A: Almost loss of activity with N-formyl-D/L-
FT methionine."
FT /evidence="ECO:0000269|PubMed:25875730"
SQ SEQUENCE 375 AA; 41757 MW; 49894E9581844BD4 CRC64;
MAINIEYVIL RHLQMELKAP FTTSFGTFQR KELILVEVVD RDGVSGWGES VAFSAPWYSE
ETVKTNWHML EDFLVPLALA EPIHHPEELS KRFSAIRQNN MAKAALEGAV WDLYAKRLGV
PLSQALGGAK KDIEVGVSIG IQPTVADLLQ VIERYVAQGY RRIKVKIKPS WDVDVIREVR
RVFPDVPLMA DANSAYTLVD ADRLKALDEF GLLMIEQPLA ADDLVDHARL QPLLQTPICL
DESIRSYDDA RKALDLGSCR IINIKIGRVG GLGEAKRIHD LCAERGAPVW CGGMLEAGVG
RAHNIAITTL ENFTLPGDTA ASSHYWERDI ITPEVEVHGG LIRVPDAPGI GYDVDRRQVE
RYTQFAKVFH RTATA
