NSAR_THET8
ID NSAR_THET8 Reviewed; 369 AA.
AC Q5SJX8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=N-succinylamino acid racemase {ECO:0000303|PubMed:24872444};
DE Short=NSAR {ECO:0000303|PubMed:24872444};
DE EC=5.1.1.- {ECO:0000269|PubMed:24872444};
DE AltName: Full=N-acylamino acid racemase {ECO:0000303|PubMed:18214979};
DE Short=NAAAR {ECO:0000303|PubMed:18214979};
DE AltName: Full=o-succinylbenzoate synthase {ECO:0000303|PubMed:24872444};
DE Short=OSB synthase {ECO:0000305};
DE Short=OSBS {ECO:0000303|PubMed:24872444};
DE EC=4.2.1.113 {ECO:0000269|PubMed:24872444};
GN OrderedLocusNames=TTHA0874 {ECO:0000312|EMBL:BAD70697.1};
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND EVOLUTION OF THE O-SUCCINYLBENZOATE SYNTHASE/N-ACYLAMINO ACID
RP RACEMASE FAMILY.
RX PubMed=16740275; DOI=10.1016/j.jmb.2006.04.055;
RA Glasner M.E., Fayazmanesh N., Chiang R.A., Sakai A., Jacobson M.P.,
RA Gerlt J.A., Babbitt P.C.;
RT "Evolution of structure and function in the o-succinylbenzoate synthase/N-
RT acylamino acid racemase family of the enolase superfamily.";
RL J. Mol. Biol. 360:228-250(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24872444; DOI=10.1073/pnas.1318703111;
RA Odokonyero D., Sakai A., Patskovsky Y., Malashkevich V.N., Fedorov A.A.,
RA Bonanno J.B., Fedorov E.V., Toro R., Agarwal R., Wang C., Ozerova N.D.,
RA Yew W.S., Sauder J.M., Swaminathan S., Burley S.K., Almo S.C.,
RA Glasner M.E.;
RT "Loss of quaternary structure is associated with rapid sequence divergence
RT in the OSBS family.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:8535-8540(2014).
RN [4] {ECO:0007744|PDB:2ZC8}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=18214979; DOI=10.1002/prot.21926;
RA Hayashida M., Kim S.H., Takeda K., Hisano T., Miki K.;
RT "Crystal structure of N-acylamino acid racemase from Thermus thermophilus
RT HB8.";
RL Proteins 71:519-523(2008).
CC -!- FUNCTION: Acts as a N-succinylamino acid racemase (NSAR) that catalyzes
CC the racemization of N-succinyl-L-phenylglycine (PubMed:24872444). Also
CC converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC)
CC to 2-succinylbenzoate (OSB) (PubMed:24872444). Catalyzes both N-
CC succinylamino acid racemization and OSB synthesis at equivalent rates
CC (PubMed:24872444). However, NSAR activity is probably the protein's
CC biological function, because menaquinone biosynthesis genes are missing
CC in this species (Probable). {ECO:0000269|PubMed:24872444,
CC ECO:0000305|PubMed:16740275}.
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:0000269|PubMed:24872444};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:24872444};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:Q44244};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=440 uM for N-succinyl-L-phenylglycine
CC {ECO:0000269|PubMed:24872444};
CC KM=9.4 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 33 sec(-1) with N-succinyl-L-phenylglycine as substrate
CC (PubMed:24872444). kcat is 6.1 sec(-1) with SHCHC as substrate
CC (PubMed:24872444). {ECO:0000269|PubMed:24872444};
CC -!- SUBUNIT: Homooctamer. Tetramer of dimers.
CC {ECO:0000269|PubMed:18214979}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008226; BAD70697.1; -; Genomic_DNA.
DR RefSeq; WP_011228259.1; NC_006461.1.
DR RefSeq; YP_144140.1; NC_006461.1.
DR PDB; 2ZC8; X-ray; 1.95 A; A/B=1-369.
DR PDBsum; 2ZC8; -.
DR SMR; Q5SJX8; -.
DR STRING; 300852.55772256; -.
DR EnsemblBacteria; BAD70697; BAD70697; BAD70697.
DR GeneID; 3168423; -.
DR KEGG; ttj:TTHA0874; -.
DR PATRIC; fig|300852.9.peg.867; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_4_0; -.
DR OMA; CRIINIK; -.
DR PhylomeDB; Q5SJX8; -.
DR EvolutionaryTrace; Q5SJX8; -.
DR Proteomes; UP000000532; 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 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 3D-structure; Isomerase; Lyase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..369
FT /note="N-succinylamino acid racemase"
FT /id="PRO_0000455104"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q44244"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q44244"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q44244"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q44244"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q44244"
FT STRAND 5..21
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2ZC8"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:2ZC8"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:2ZC8"
SQ SEQUENCE 369 AA; 41018 MW; A6E02DCA1DA3F084 CRC64;
MRIEAAELRI LELPLKFRFE TSFGVQTKRT ILLLRLFGEG LEGLGEGVME RLPLYREETV
AGARYLLEEV FLPRVLGRDL PNPEALREAL APFRGNPMAK AVLEMAFFDL WAKALGRPLW
QVLGGVRQAV EVGVSLGIQP SVEDTLRVVE RHLEEGYRRI KLKIKPGWDY EVLKAVREAF
PEATLTADAN SAYSLANLAQ LKRLDELRLD YIEQPLAYDD LLDHAKLQRE LSTPICLDES
LTGAEKARKA IELGAGRVFN VKPARLGGHG ESLRVHALAE SAGIPLWMGG MLEAGVGRAH
NLHLATLPGF TKPGDVSSAS RYWEEDIVEE ALEAKDGLMP VPEGVGIGVH LKLPFVERVT
LWQRYMSAS
