NSAR_AMYSP
ID NSAR_AMYSP Reviewed; 368 AA.
AC Q44244;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=N-succinylamino acid racemase {ECO:0000303|PubMed:24955846};
DE Short=NSAR {ECO:0000303|PubMed:24955846};
DE EC=5.1.1.- {ECO:0000269|PubMed:14705949, ECO:0000269|PubMed:24955846};
DE AltName: Full=N-acylamino acid racemase {ECO:0000303|PubMed:7766089};
DE Short=AAR {ECO:0000303|PubMed:7766089};
DE Short=NAAAR {ECO:0000303|PubMed:10194342};
DE EC=5.1.1.- {ECO:0000269|PubMed:10194342, ECO:0000269|PubMed:14705949, ECO:0000269|PubMed:23130969, ECO:0000269|PubMed:7766084};
DE AltName: Full=o-succinylbenzoate synthase {ECO:0000303|PubMed:10194342};
DE Short=OSB synthase {ECO:0000305};
DE Short=OSBS {ECO:0000303|PubMed:10194342};
DE EC=4.2.1.113 {ECO:0000269|PubMed:10194342, ECO:0000269|PubMed:14705949, ECO:0000269|PubMed:24955846};
GN Name=Aaar {ECO:0000312|EMBL:BAA06400.1};
OS Amycolatopsis sp.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis; unclassified Amycolatopsis.
OX NCBI_TaxID=37632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TS-1-60;
RX PubMed=7766089; DOI=10.1007/s002530050347;
RA Tokuyama S., Hatano K.;
RT "Cloning, DNA sequencing and heterologous expression of the gene for
RT thermostable N-acylamino acid racemase from Amycolatopsis sp. TS-1-60 in
RT Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 42:884-889(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-24, FUNCTION AS A RACEMASE, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=TS-1-60;
RX PubMed=7766084; DOI=10.1007/bf00191181;
RA Tokuyama S., Hatano K.;
RT "Purification and properties of thermostable N-acylamino acid racemase from
RT Amycolatopsis sp. TS-1-60.";
RL Appl. Microbiol. Biotechnol. 42:853-859(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LYS-163 AND LYS-263.
RC STRAIN=TS-1-60;
RX PubMed=10194342; DOI=10.1021/bi990140p;
RA Palmer D.R., Garrett J.B., Sharma V., Meganathan R., Babbitt P.C.,
RA Gerlt J.A.;
RT "Unexpected divergence of enzyme function and sequence: 'N-acylamino acid
RT racemase' is o-succinylbenzoate synthase.";
RL Biochemistry 38:4252-4258(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES,
RP AND MUTAGENESIS OF LYS-163 AND LYS-263.
RC STRAIN=TS-1-60;
RX PubMed=14705949; DOI=10.1021/bi035815+;
RA Taylor Ringia E.A., Garrett J.B., Thoden J.B., Holden H.M., Rayment I.,
RA Gerlt J.A.;
RT "Evolution of enzymatic activity in the enolase superfamily: functional
RT studies of the promiscuous o-succinylbenzoate synthase from
RT Amycolatopsis.";
RL Biochemistry 43:224-229(2004).
RN [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF PRO-18; PHE-19; ARG-20; THR-21; SER-22; PHE-23; GLY-24 AND
RP ASP-140.
RC STRAIN=TS-1-60;
RX PubMed=24955846; DOI=10.1021/bi500573v;
RA McMillan A.W., Lopez M.S., Zhu M., Morse B.C., Yeo I.C., Amos J., Hull K.,
RA Romo D., Glasner M.E.;
RT "Role of an active site loop in the promiscuous activities of Amycolatopsis
RT sp. T-1-60 NSAR/OSBS.";
RL Biochemistry 53:4434-4444(2014).
RN [7] {ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB, ECO:0007744|PDB:1SJC, ECO:0007744|PDB:1SJD}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEXES WITH 2-SUCCINYLBENZOIC
RP ACID; N-ACETYL-METHIONINE; N-SUCCINYL-METHIONINE; N-SUCCINYL-PHENYLGLYCINE
RP AND MAGNESIUM, COFACTOR, SUBUNIT, DOMAIN, AND ACTIVE SITES.
RC STRAIN=TS-1-60;
RX PubMed=15134446; DOI=10.1021/bi0497897;
RA Thoden J.B., Taylor Ringia E.A., Garrett J.B., Gerlt J.A., Holden H.M.,
RA Rayment I.;
RT "Evolution of enzymatic activity in the enolase superfamily: structural
RT studies of the promiscuous o-succinylbenzoate synthase from
RT Amycolatopsis.";
RL Biochemistry 43:5716-5727(2004).
RN [8] {ECO:0007744|PDB:4A6G}
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF MUTANT ASP-291/TYR-323 IN COMPLEX
RP WITH N-ACETYL-METHIONINE AND MAGNESIUM, FUNCTION AS A RACEMASE, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, AND MUTAGENESIS OF
RP GLY-291 AND PHE-323.
RC STRAIN=TS-1-60;
RX PubMed=23130969; DOI=10.1021/ja305438y;
RA Baxter S., Royer S., Grogan G., Brown F., Holt-Tiffin K.E., Taylor I.N.,
RA Fotheringham I.G., Campopiano D.J.;
RT "An improved racemase/acylase biotransformation for the preparation of
RT enantiomerically pure amino acids.";
RL J. Am. Chem. Soc. 134:19310-19313(2012).
RN [9] {ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP, ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT, ECO:0007744|PDB:5FJU}
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF MUTANTS IN COMPLEXES WITH
RP N-ACETYL NAPHTHYLALANINE; N-ACETYL PHENYLALANINE AND MAGNESIUM.
RC STRAIN=TS-1-60;
RA Sanchez-Carron G., Campopiano D., Grogan G.;
RT "Structure of N-Acylamino Acid Racemase Mutants in Complex with
RT Substrates.";
RL Submitted (OCT-2015) to the PDB data bank.
CC -!- FUNCTION: Acts as a N-succinylamino acid racemase (NSAR) that catalyzes
CC the racemization of N-succinyl-phenylglycine and N-succinyl-methionine
CC (PubMed:14705949, PubMed:24955846). Can catalyze the racemization of a
CC broad range of N-acylamino acids, including N-acetyl-D/L-methionine, N-
CC propionyl-D/L-methionine, N-butyryl-D/L-methionine and N-chloroacetyl-
CC L-valine (PubMed:7766084, PubMed:10194342, PubMed:14705949,
CC PubMed:23130969). Also converts 2-succinyl-6-hydroxy-2,4-
CC cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB)
CC (PubMed:10194342, PubMed:14705949, PubMed:24955846). Catalyzes both N-
CC succinylamino acid racemization and OSB synthesis at equivalent rates
CC (PubMed:14705949, PubMed:24955846). NSAR is probably the biological
CC function of this enzyme (Probable). {ECO:0000269|PubMed:10194342,
CC ECO:0000269|PubMed:14705949, ECO:0000269|PubMed:23130969,
CC ECO:0000269|PubMed:24955846, ECO:0000269|PubMed:7766084,
CC ECO:0000305|PubMed:16740275, ECO:0000305|PubMed:24955846}.
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:10194342, ECO:0000269|PubMed:14705949,
CC ECO:0000269|PubMed:23130969, ECO:0000269|PubMed:7766084};
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:10194342, ECO:0000269|PubMed:14705949,
CC ECO:0000269|PubMed:24955846};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:7766084};
CC Note=Binds 1 divalent metal cation per subunit (PubMed:15134446).
CC Enhanced by the addition of divalent metal ions such as Co(2+), Mn(2+)
CC and Fe(2+) (PubMed:7766084). {ECO:0000269|PubMed:15134446,
CC ECO:0000269|PubMed:7766084};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and sulfhydryl reagents such as
CC p-chloromercuribenzoic acid (PubMed:7766084). Both OSBS and NAAAR
CC activities are inhibited competitively by salicylhydroxamate
CC (PubMed:10194342). {ECO:0000269|PubMed:10194342,
CC ECO:0000269|PubMed:7766084}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 mM for N-succinyl-R-methionine {ECO:0000269|PubMed:14705949};
CC KM=5.9 mM for N-succinyl-S-methionine {ECO:0000269|PubMed:14705949};
CC KM=0.94 mM for N-succinyl-R-phenylglycine
CC {ECO:0000269|PubMed:14705949};
CC KM=0.95 mM for N-succinyl-S-phenylglycine
CC {ECO:0000269|PubMed:14705949};
CC KM=1 mM for N-succinyl-L-phenylglycine {ECO:0000269|PubMed:24955846};
CC KM=18.5 mM for N-acetyl-L-methionine {ECO:0000269|PubMed:7766084};
CC KM=18 mM for N-acetyl-L-methionine {ECO:0000269|PubMed:23130969};
CC KM=11.3 mM for N-acetyl-D-methionine {ECO:0000269|PubMed:7766084};
CC KM=40 mM for N-acetyl-D-methionine {ECO:0000269|PubMed:23130969};
CC KM=9.8 mM for N-acetyl-R-methionine {ECO:0000269|PubMed:14705949};
CC KM=11 mM for N-acetyl-S-methionine {ECO:0000269|PubMed:14705949};
CC KM=35 mM for N-acetyl-D-(4-fluoro)phenylglycine
CC {ECO:0000269|PubMed:23130969};
CC KM=0.48 mM for SHCHC {ECO:0000269|PubMed:14705949};
CC KM=0.55 mM for SHCHC {ECO:0000269|PubMed:24955846};
CC Note=kcat is 110 sec(-1) with N-succinyl-R/S-methionine as substrate
CC (PubMed:14705949). kcat is 190 sec(-1) with N-succinyl-R/S-
CC phenylglycine as substrate (PubMed:14705949). kcat is 42 sec(-1) with
CC N-succinyl-L-phenylglycine as substrate (PubMed:24955846). kcat is 20
CC sec(-1) with N-acetyl-L-methionine as substrate (PubMed:23130969).
CC kcat is 14 sec(-1) with N-acetyl-D-methionine as substrate
CC (PubMed:23130969). kcat is 4.8 sec(-1) with N-acetyl-R-methionine as
CC substrate (PubMed:14705949). kcat is 6.4 sec(-1) with N-acetyl-S-
CC methionine as substrate (PubMed:14705949). kcat is 11.7 sec(-1) with
CC N-acetyl-S-methionine as substrate (PubMed:10194342). kcat is 41
CC sec(-1) with N-acetyl-D-(4-fluoro)phenylglycine as substrate
CC (PubMed:23130969). kcat is 97 sec(-1) with N-acetyl-allylglycine as
CC substrate (PubMed:23130969). kcat is 120 sec(-1) with SHCHC as
CC substrate (PubMed:10194342, PubMed:14705949). kcat is 46 sec(-1) with
CC SHCHC as substrate (PubMed:24955846). {ECO:0000269|PubMed:10194342,
CC ECO:0000269|PubMed:14705949, ECO:0000269|PubMed:23130969,
CC ECO:0000269|PubMed:24955846};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:7766084};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Stable at 55 degrees
CC Celsius for 30 min. {ECO:0000269|PubMed:7766084};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:15134446,
CC ECO:0000269|PubMed:7766084}.
CC -!- DOMAIN: The active-site cavity can accommodate both the hydrophobic
CC substrate for the OSBS reaction and the substrates for the racemase
CC activity. Accommodation of the components of the N-acyl linkage appears
CC to be the reason that this enzyme is capable of a racemization reaction
CC on these substrates, whereas the orthologous OSBS from E.coli lacks
CC this functionality. {ECO:0000269|PubMed:15134446}.
CC -!- BIOTECHNOLOGY: Variants with increased racemase activity could be used
CC on an industrial scale for the production of enantiomerically pure
CC alpha-amino acids. {ECO:0000269|PubMed:23130969}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000305}.
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DR EMBL; D30738; BAA06400.1; -; Genomic_DNA.
DR PIR; I39598; I39598.
DR PDB; 1SJA; X-ray; 2.30 A; A/B/C/D=1-368.
DR PDB; 1SJB; X-ray; 2.20 A; A/B/C/D=1-368.
DR PDB; 1SJC; X-ray; 2.10 A; A/B/C/D=1-368.
DR PDB; 1SJD; X-ray; 1.87 A; A/B/C/D=1-368.
DR PDB; 4A6G; X-ray; 2.71 A; A/B/C/D=1-368.
DR PDB; 5FJO; X-ray; 2.08 A; A/B=1-368.
DR PDB; 5FJP; X-ray; 2.58 A; A/B/C/D=1-368.
DR PDB; 5FJR; X-ray; 2.44 A; A/B/C/D=1-368.
DR PDB; 5FJT; X-ray; 2.11 A; A/B/C/D=1-368.
DR PDB; 5FJU; X-ray; 2.52 A; A/B/C/D=1-368.
DR PDB; 7S8W; X-ray; 2.90 A; A/B/C/D=1-368.
DR PDBsum; 1SJA; -.
DR PDBsum; 1SJB; -.
DR PDBsum; 1SJC; -.
DR PDBsum; 1SJD; -.
DR PDBsum; 4A6G; -.
DR PDBsum; 5FJO; -.
DR PDBsum; 5FJP; -.
DR PDBsum; 5FJR; -.
DR PDBsum; 5FJT; -.
DR PDBsum; 5FJU; -.
DR PDBsum; 7S8W; -.
DR SMR; Q44244; -.
DR DrugBank; DB01646; N-Acetylmethionine.
DR DrugBank; DB04511; N-Succinyl Methionine.
DR DrugBank; DB03299; N-Succinyl Phenylglycine.
DR DrugBank; DB02251; O-Succinylbenzoate.
DR BRENDA; 4.2.1.113; 316.
DR SABIO-RK; Q44244; -.
DR EvolutionaryTrace; Q44244; -.
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; Direct protein sequencing; Isomerase; Lyase; Magnesium;
KW Metal-binding.
FT CHAIN 1..368
FT /note="N-succinylamino acid racemase"
FT /id="PRO_0000455102"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:14705949,
FT ECO:0000305|PubMed:15134446"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:14705949,
FT ECO:0000305|PubMed:15134446"
FT BINDING 135
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0007744|PDB:1SJB"
FT BINDING 161..163
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0007744|PDB:1SJB"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0000269|PubMed:23130969, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB,
FT ECO:0007744|PDB:1SJC, ECO:0007744|PDB:4A6G,
FT ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP,
FT ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT,
FT ECO:0007744|PDB:5FJU"
FT BINDING 191
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0007744|PDB:1SJB"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0000269|PubMed:23130969, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB,
FT ECO:0007744|PDB:1SJC, ECO:0007744|PDB:4A6G,
FT ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP,
FT ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT,
FT ECO:0007744|PDB:5FJU"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0000269|PubMed:23130969, ECO:0000269|Ref.9,
FT ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB,
FT ECO:0007744|PDB:1SJC, ECO:0007744|PDB:4A6G,
FT ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP,
FT ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT,
FT ECO:0007744|PDB:5FJU"
FT BINDING 293
FT /ligand="2-succinylbenzoate"
FT /ligand_id="ChEBI:CHEBI:18325"
FT /evidence="ECO:0000269|PubMed:15134446,
FT ECO:0007744|PDB:1SJB"
FT MUTAGEN 18
FT /note="P->A: Small increase in OSBS catalytic efficiency
FT and 2-fold decrease in NSAR catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 19
FT /note="F->A: 200-fold decrease in OSBS catalytic efficiency
FT and 120-fold decrease in NSAR catalytic efficiency. 2100-
FT fold decrease in OSBS catalytic efficiency and 180-fold
FT decrease in NSAR catalytic efficiency; when associated with
FT A-23."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 20
FT /note="R->E: 32-fold decrease in OSBS catalytic efficiency
FT and 8-fold decrease in NSAR catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 21
FT /note="T->A: 4-fold decrease in OSBS and NSAR catalytic
FT efficiencies."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 22
FT /note="S->R: 3-fold increase in OSBS catalytic efficiency
FT and 4-fold decrease in NSAR catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 23
FT /note="F->A: 2100-fold decrease in OSBS catalytic
FT efficiency and 180-fold decrease in NSAR catalytic
FT efficiency; when associated with A-19."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 24
FT /note="G->A: Small decrease in OSBS catalytic efficiency
FT and 4-fold decrease in NSAR catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 140
FT /note="D->R: 3-fold decrease in OSBS and NSAR catalytic
FT efficiencies."
FT /evidence="ECO:0000269|PubMed:24955846"
FT MUTAGEN 163
FT /note="K->A,R,S: Significantly impairs both NAAAR and OSBS
FT activities."
FT /evidence="ECO:0000269|PubMed:10194342,
FT ECO:0000269|PubMed:14705949"
FT MUTAGEN 263
FT /note="K->R,S: Significantly impairs both NAAAR and OSBS
FT activities."
FT /evidence="ECO:0000269|PubMed:10194342,
FT ECO:0000269|PubMed:14705949"
FT MUTAGEN 291
FT /note="G->D: Shows up to 6-fold higher activity than the
FT wild-type on a range of N-acetylated amino acids; when
FT associated with Y-323."
FT /evidence="ECO:0000269|PubMed:23130969"
FT MUTAGEN 323
FT /note="F->Y: Shows up to 6-fold higher activity than the
FT wild-type on a range of N-acetylated amino acids; when
FT associated with D-291."
FT /evidence="ECO:0000269|PubMed:23130969"
FT CONFLICT 23
FT /note="F -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..21
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 24..37
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1SJD"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:4A6G"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:1SJD"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:1SJD"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:1SJD"
SQ SEQUENCE 368 AA; 39406 MW; 623A27548DA0E8C4 CRC64;
MKLSGVELRR VQMPLVAPFR TSFGTQSVRE LLLLRAVTPA GEGWGECVTM AGPLYSSEYN
DGAEHVLRHY LIPALLAAED ITAAKVTPLL AKFKGHRMAK GALEMAVLDA ELRAHERSFA
AELGSVRDSV PCGVSVGIMD TIPQLLDVVG GYLDEGYVRI KLKIEPGWDV EPVRAVRERF
GDDVLLQVDA NTAYTLGDAP QLARLDPFGL LLIEQPLEEE DVLGHAELAR RIQTPICLDE
SIVSARAAAD AIKLGAVQIV NIKPGRVGGY LEARRVHDVC AAHGIPVWCG GMIETGLGRA
ANVALASLPN FTLPGDTSAS DRFYKTDITE PFVLSGGHLP VPTGPGLGVA PIPELLDEVT
TAKVWIGS
