NSAR_BACCR
ID NSAR_BACCR Reviewed; 369 AA.
AC Q81IL5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=N-succinyl-L-Arg/Lys racemase;
DE EC=5.1.1.-;
DE AltName: Full=N-succinyl amino acid racemase;
DE Short=NSAR;
GN OrderedLocusNames=BC_0371;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH N-SUCCINYL LYSINE
RP AND MAGNESIUM, FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=17603539; DOI=10.1038/nchembio.2007.11;
RA Song L., Kalyanaraman C., Fedorov A.A., Fedorov E.V., Glasner M.E.,
RA Brown S., Imker H.J., Babbitt P.C., Almo S.C., Jacobson M.P., Gerlt J.A.;
RT "Prediction and assignment of function for a divergent N-succinyl amino
RT acid racemase.";
RL Nat. Chem. Biol. 3:486-491(2007).
CC -!- FUNCTION: Catalyzes efficient racemization of N-succinyl-L-Arg and N-
CC succinyl-L-Lys, suggesting that these are physiological substrates of
CC this enzyme. Has low activity with L-Asp-L-Lys, and even lower activity
CC with L-Leu-L-Arg, L-Leu-L-Lys, N-succinyl-L-His and N-succinyl-L-Met
CC (in vitro). {ECO:0000269|PubMed:17603539}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17603539};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17603539};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 mM for N-succinyl-L-Arg {ECO:0000269|PubMed:17603539};
CC KM=3.0 mM for N-succinyl-L-Met {ECO:0000269|PubMed:17603539};
CC KM=11 mM for N-succinyl-L-His {ECO:0000269|PubMed:17603539};
CC KM=1.2 mM for L-Leu-L-Lys {ECO:0000269|PubMed:17603539};
CC KM=3.9 mM for L-Asp-L-Lys {ECO:0000269|PubMed:17603539};
CC KM=16 mM for L-Leu-L-Arg {ECO:0000269|PubMed:17603539};
CC -!- MISCELLANEOUS: Part of a large, functionally divergent protein family.
CC Protein modeling and substrate docking was used to predict the
CC substrate specificity, prior to biochemical analysis.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. {ECO:0000305}.
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DR EMBL; AE016877; AAP07411.1; -; Genomic_DNA.
DR RefSeq; NP_830210.1; NC_004722.1.
DR RefSeq; WP_000704492.1; NZ_CP034551.1.
DR PDB; 2P88; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-369.
DR PDB; 2P8B; X-ray; 1.70 A; A=1-369.
DR PDB; 2P8C; X-ray; 2.00 A; A=1-369.
DR PDBsum; 2P88; -.
DR PDBsum; 2P8B; -.
DR PDBsum; 2P8C; -.
DR AlphaFoldDB; Q81IL5; -.
DR SMR; Q81IL5; -.
DR STRING; 226900.BC_0371; -.
DR EnsemblBacteria; AAP07411; AAP07411; BC_0371.
DR KEGG; bce:BC0371; -.
DR PATRIC; fig|226900.8.peg.343; -.
DR HOGENOM; CLU_030273_4_0_9; -.
DR OMA; HEEFPVT; -.
DR SABIO-RK; Q81IL5; -.
DR EvolutionaryTrace; Q81IL5; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0036361; F:racemase activity, acting on amino acids and derivatives; IDA:CACAO.
DR GO; GO:0016854; F:racemase and epimerase activity; IDA:UniProtKB.
DR GO; GO:0006518; P:peptide metabolic process; IDA:UniProtKB.
DR CDD; cd03319; L-Ala-DL-Glu_epimerase; 1.
DR Gene3D; 3.20.20.120; -; 1.
DR Gene3D; 3.30.390.10; -; 1.
DR InterPro; IPR034603; Dipeptide_epimerase.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..369
FT /note="N-succinyl-L-Arg/Lys racemase"
FT /id="PRO_0000429658"
FT BINDING 26
FT /ligand="substrate"
FT BINDING 51
FT /ligand="substrate"
FT BINDING 161..163
FT /ligand="substrate"
FT BINDING 191..193
FT /ligand="substrate"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17603539"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17603539"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17603539"
FT BINDING 267
FT /ligand="substrate"
FT BINDING 295..296
FT /ligand="substrate"
FT BINDING 320..322
FT /ligand="substrate"
FT STRAND 3..21
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 24..38
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 168..182
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2P8B"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:2P8C"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 300..310
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:2P8B"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:2P8B"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:2P8B"
SQ SEQUENCE 369 AA; 40949 MW; 26D38191EC5D0450 CRC64;
MKITAIHLYA IRLPLRNPFV ISYGSYSDMP SIIVKMETDE GIIGYGEGVA DDHVTGESWE
STFHTLKHTL TPALIGQNPM NIEKIHDMMD NTIYGVPTAK AAIDIACFDI MGKKLNQPVY
QLIGGRYHEE FPVTHVLSIA DPENMAEEAA SMIQKGYQSF KMKVGTNVKE DVKRIEAVRE
RVGNDIAIRV DVNQGWKNSA NTLTALRSLG HLNIDWIEQP VIADDIDAMA HIRSKTDLPL
MIDEGLKSSR EMRQIIKLEA ADKVNIKLMK CGGIYPAVKL AHQAEMAGIE CQVGSMVESS
VASSAGFHVA FSKKIITSVE LTGPLKFTKD IGNLHYDVPF IRLNEKPGLG IEINEDTLQE
LTVFQDIVR
