MENC_GEOKU
ID MENC_GEOKU Reviewed; 375 AA.
AC B1A612;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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:0000303|Ref.1};
DE Short=NAAAR {ECO:0000303|Ref.1};
DE AltName: Full=N-succinylamino acid racemase {ECO:0000303|Ref.1};
DE Short=NSAAR {ECO:0000303|Ref.1};
DE Short=NSAR {ECO:0000305};
DE EC=5.1.1.- {ECO:0000269|PubMed:25875730, ECO:0000269|Ref.1};
DE AltName: Full=o-succinylbenzoic acid synthase {ECO:0000255|HAMAP-Rule:MF_01933};
GN Name=menC {ECO:0000255|HAMAP-Rule:MF_01933};
GN Synonyms=nsaar {ECO:0000303|Ref.1};
OS Geobacillus kaustophilus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=CECT4264;
RX DOI=10.1016/j.procbio.2009.03.020;
RA Pozo-Dengra J., Martinez-Gomez A.I., Martinez-Rodriguez S.,
RA Clemente-Jimenez J.M., Rodriguez-Vico F., Las Heras-Vazquez F.J.;
RT "Racemization study on different N-acetylamino acids by a recombinant N-
RT succinylamino acid racemase from Geobacillus kaustophilus CECT4264.";
RL Process Biochem. 44:835-841(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CECT4264;
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 various N-succinylamino acids, including N-succinyl-
CC alanine and N-succinyl-phenylalanine (Ref.1). Can catalyze the
CC racemization of a broad range of N-acylamino acids, including N-acetyl-
CC methionine, N-acetyl-phenylalanine, N-carbamoyl-methionine, N-formyl-D-
CC methionine, N-formyl-D-norleucine and N-carbamoyl-D-norleucine (Ref.1,
CC PubMed:25875730). May be a bifunctional enzyme involved in menaquinone
CC biosynthesis and in an irreversible pathway for the conversion of D- to
CC L-amino acids, thereby facilitating the survival and/or growth of the
CC organism (By similarity). {ECO:0000250|UniProtKB:Q5L1G9,
CC ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|PubMed:25875730,
CC ECO:0000269|Ref.1}.
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, ECO:0000269|Ref.1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-phenylalanine = N-acetyl-L-phenylalanine;
CC Xref=Rhea:RHEA:62772, ChEBI:CHEBI:57702, ChEBI:CHEBI:143878;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01933, ECO:0000269|Ref.1};
CC Note=Shows highest activity in vitro with Co(2+), Mn(2+) and Ni(2+).
CC {ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for N-succinyl-L-alanine {ECO:0000269|Ref.1};
CC KM=0.13 mM for N-succinyl-D-alanine {ECO:0000269|Ref.1};
CC KM=0.13 mM for N-succinyl-L-phenylalanine {ECO:0000269|Ref.1};
CC KM=0.04 mM for N-succinyl-D-phenylalanine {ECO:0000269|Ref.1};
CC KM=8 mM for N-acetyl-L-methionine {ECO:0000269|Ref.1};
CC KM=7 mM for N-acetyl-D-methionine {ECO:0000269|Ref.1};
CC KM=43 mM for N-acetyl-L-phenylalanine {ECO:0000269|Ref.1};
CC KM=23 mM for N-acetyl-D-phenylalanine {ECO:0000269|Ref.1};
CC KM=5 mM for N-carbamoyl-L-methionine {ECO:0000269|Ref.1};
CC KM=2 mM for N-carbamoyl-D-methionine {ECO:0000269|Ref.1};
CC Note=kcat is 43 sec(-1) with N-succinyl-L-alanine as substrate. kcat
CC is 15 sec(-1) with N-succinyl-D-alanine as substrate. kcat is 5 sec(-
CC 1) with N-succinyl-L-phenylalanine as substrate. kcat is 2 sec(-1)
CC with N-succinyl-D-phenylalanine as substrate. kcat is 22 sec(-1) with
CC N-acetyl-L-methionine as substrate. kcat is 20 sec(-1) with N-acetyl-
CC D-methionine as substrate. kcat is 16 sec(-1) with N-acetyl-L-
CC phenylalanine as substrate. kcat is 10 sec(-1) with N-acetyl-D-
CC phenylalanine as substrate. kcat is 2 sec(-1) with N-carbamoyl-L-
CC methionine as substrate. kcat is 2 sec(-1) with N-carbamoyl-D-
CC methionine as substrate. {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.1};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. {ECO:0000269|Ref.1};
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|Ref.1}.
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; EU427322; ABZ81711.1; -; Genomic_DNA.
DR SMR; B1A612; -.
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_0000455097"
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; 42004 MW; 203E9FF25527B830 CRC64;
MAINIEYVIL RHLQMELKAP FTTSFGTFQT KEFILVEVVD CDGVSGWGES VAFSVPWYSE
ETVKTNWHML EEFLVPLLFS KPLRHPAELP ERFAAIRQNN MAKAALEGAV WDLYAKRLGV
PLCQALGGTK KEIEVGVSIG IQPTVDDLLQ VIERYVAQGY RRIKVKIKPG WDVDVIRDVR
RAFPDVPLMA DANSAYTLAD AKRLQALDEF GLMMIEQPLA ADDLVDHARL QPLLKTPICL
DESIRSYDDA RKALDLGSCR IINIKIGRVG GLWEAKRIHD LCAERGVPVW CGGMLEAGVG
RAHNIAITTL ENFALPGDTA ASSHYWERDI ITPEVEVHNG LIRVPNAPGI GYDVDRRQVE
RYTQFAKLFH RTATA
