NSAR_DEIRA
ID NSAR_DEIRA Reviewed; 375 AA.
AC Q9RYA6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=N-succinylamino acid racemase {ECO:0000303|PubMed:24872444};
DE Short=NSAAR {ECO:0000303|PubMed:25875730};
DE Short=NSAR {ECO:0000303|PubMed:24872444};
DE EC=5.1.1.- {ECO:0000269|PubMed:24872444, ECO:0000269|PubMed:25875730};
DE AltName: Full=N-acylamino acid racemase {ECO:0000303|PubMed:15313614};
DE Short=NAAAR {ECO:0000303|PubMed:15313614};
DE EC=5.1.1.- {ECO:0000269|PubMed:15313614, ECO:0000269|PubMed:16650857, ECO:0000269|PubMed:25875730};
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=DR_0044 {ECO:0000312|EMBL:AAF09631.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=CECT833;
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).
RN [5] {ECO:0007744|PDB:1R0M, ECO:0007744|PDB:1XPY, ECO:0007744|PDB:1XS2}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP MAGNESIUM AND N-ACETYL-L-GLUTAMINE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, BIOTECHNOLOGY,
RP AND ACTIVE SITES.
RX PubMed=15313614; DOI=10.1016/j.jmb.2004.07.023;
RA Wang W.C., Chiu W.C., Hsu S.K., Wu C.L., Chen C.Y., Liu J.S., Hsu W.H.;
RT "Structural basis for catalytic racemization and substrate specificity of
RT an N-acylamino acid racemase homologue from Deinococcus radiodurans.";
RL J. Mol. Biol. 342:155-169(2004).
RN [6] {ECO:0007744|PDB:2FKP, ECO:0007744|PDB:2GGG, ECO:0007744|PDB:2GGH, ECO:0007744|PDB:2GGI, ECO:0007744|PDB:2GGJ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANTS CYS-68/CYS-72;
RP CYS-149/CYS-182; CYS-127/CYS-313 AND CYS-218, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, BIOTECHNOLOGY, AND MUTAGENESIS OF
RP VAL-48; MET-56; PRO-60; GLU-65; ALA-68; ASP-72; TYR-100; ARG-120; GLY-127;
RP GLU-149; GLY-163; ALA-182; TYR-218; VAL-265; THR-313 AND ASP-343.
RX PubMed=16650857; DOI=10.1016/j.jmb.2006.03.063;
RA Chiu W.C., You J.Y., Liu J.S., Hsu S.K., Hsu W.H., Shih C.H., Hwang J.K.,
RA Wang W.C.;
RT "Structure-stability-activity relationship in covalently cross-linked N-
RT carbamoyl D-amino acid amidohydrolase and N-acylamino acid racemase.";
RL J. Mol. Biol. 359:741-753(2006).
CC -!- FUNCTION: Acts as a N-succinylamino acid racemase (NSAR) that catalyzes
CC the racemization of N-succinyl-L-phenylglycine and N-succinyl-D/L-
CC phenylalanine (PubMed:24872444, PubMed:25875730). Can catalyze the
CC racemization of a broad range of N-acylamino acids, including N-acetyl-
CC D/L-methionine, N-acetyl-D/L-phenylalanine, N-acetyl-L-glutamine, N-
CC acetyl-L-tryptophan, N-acetyl-L-leucine, N-formyl-D-methionine, N-
CC formyl-D-norleucine, N-carbamoyl-D-methionine and N-carbamoyl-D-
CC norleucine (PubMed:15313614, PubMed:16650857, PubMed:25875730). 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:15313614,
CC ECO:0000269|PubMed:16650857, ECO:0000269|PubMed:24872444,
CC ECO:0000269|PubMed:25875730, ECO:0000305|PubMed:16740275}.
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:15313614, ECO:0000269|PubMed:16650857};
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|PubMed:15313614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-glutamine = N-acetyl-D-glutamine;
CC Xref=Rhea:RHEA:67988, ChEBI:CHEBI:143879, ChEBI:CHEBI:143880;
CC Evidence={ECO:0000269|PubMed:15313614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-tryptophan = N-acetyl-D-tryptophan;
CC Xref=Rhea:RHEA:60568, ChEBI:CHEBI:57877, ChEBI:CHEBI:143877;
CC Evidence={ECO:0000269|PubMed:15313614};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-L-leucine = N-acetyl-D-leucine; Xref=Rhea:RHEA:67984,
CC ChEBI:CHEBI:58270, ChEBI:CHEBI:145946;
CC Evidence={ECO:0000269|PubMed:15313614};
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:0000269|PubMed:15313614};
CC -!- ACTIVITY REGULATION: Inhibited by salicyl hydroxamate, an inhibitor of
CC o-succinylbenzoate synthase. {ECO:0000269|PubMed:15313614}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for N-succinyl-L-phenylglycine
CC {ECO:0000269|PubMed:24872444};
CC KM=24.8 mM for N-acetyl-D-methionine {ECO:0000269|PubMed:15313614};
CC KM=12.3 mM for N-acetyl-L-methionine {ECO:0000269|PubMed:15313614};
CC KM=10.6 mM for N-acetyl-L-methionine {ECO:0000269|PubMed:16650857};
CC KM=26 uM for SHCHC {ECO:0000269|PubMed:24872444};
CC Note=kcat is 520 sec(-1) with N-succinyl-L-phenylglycine as substrate
CC (PubMed:24872444). kcat is 8.5 min(-1) with N-acetyl-D-methionine as
CC substrate (PubMed:15313614). kcat is 9.9 min(-1) with N-acetyl-L-
CC methionine as substrate (PubMed:15313614). kcat is 6.85 min(-1) with
CC N-acetyl-L-methionine as substrate (PubMed:16650857). kcat is 8.1
CC sec(-1) with SHCHC as substrate (PubMed:24872444).
CC {ECO:0000269|PubMed:15313614, ECO:0000269|PubMed:16650857,
CC ECO:0000269|PubMed:24872444};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15313614};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. Stable at 55 degrees
CC Celsius. Retains 80% of activity at 70 degrees Celsius.
CC {ECO:0000269|PubMed:15313614};
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:15313614,
CC ECO:0000269|PubMed:16650857}.
CC -!- BIOTECHNOLOGY: Can be used in concert with an aminoacylase to produce
CC enantiopure alpha-amino acids, a process that has potential industrial
CC applications (PubMed:15313614). Introduction of inter-subunit S-S
CC bridges is a feasible and robust approach to increase the
CC thermostability of the enzyme without losing catalytic efficiency as
CC long as the active-site remains viable (PubMed:16650857).
CC {ECO:0000269|PubMed:15313614, ECO:0000269|PubMed:16650857}.
CC -!- SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing
CC enzyme family. MenC type 2 subfamily. {ECO:0000305}.
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DR EMBL; AE000513; AAF09631.1; -; Genomic_DNA.
DR PIR; D75568; D75568.
DR RefSeq; NP_293770.1; NC_001263.1.
DR RefSeq; WP_010886692.1; NZ_CP015081.1.
DR PDB; 1R0M; X-ray; 1.30 A; A/B/C/D=1-375.
DR PDB; 1XPY; X-ray; 2.30 A; A/B/C/D=1-375.
DR PDB; 1XS2; X-ray; 2.30 A; A/B/C/D=1-375.
DR PDB; 2FKP; X-ray; 2.00 A; A/B/C/D=1-375.
DR PDB; 2GGG; X-ray; 2.40 A; A/B/C/D=1-375.
DR PDB; 2GGH; X-ray; 2.20 A; A/B/C/D=1-375.
DR PDB; 2GGI; X-ray; 2.20 A; A/B/C/D=1-375.
DR PDB; 2GGJ; X-ray; 2.50 A; A/B/C/D=1-375.
DR PDBsum; 1R0M; -.
DR PDBsum; 1XPY; -.
DR PDBsum; 1XS2; -.
DR PDBsum; 2FKP; -.
DR PDBsum; 2GGG; -.
DR PDBsum; 2GGH; -.
DR PDBsum; 2GGI; -.
DR PDBsum; 2GGJ; -.
DR SMR; Q9RYA6; -.
DR STRING; 243230.DR_0044; -.
DR DrugBank; DB04167; Aceglutamide.
DR EnsemblBacteria; AAF09631; AAF09631; DR_0044.
DR KEGG; dra:DR_0044; -.
DR PATRIC; fig|243230.17.peg.209; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_4_4_0; -.
DR InParanoid; Q9RYA6; -.
DR OMA; CRIINIK; -.
DR OrthoDB; 951991at2; -.
DR EvolutionaryTrace; Q9RYA6; -.
DR Proteomes; UP000002524; Chromosome I.
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..375
FT /note="N-succinylamino acid racemase"
FT /id="PRO_0000455103"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15313614"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15313614"
FT BINDING 142
FT /ligand="N-acetyl-L-glutamine"
FT /ligand_id="ChEBI:CHEBI:143879"
FT /evidence="ECO:0000269|PubMed:15313614,
FT ECO:0007744|PDB:1XPY"
FT BINDING 168..170
FT /ligand="N-acetyl-L-glutamine"
FT /ligand_id="ChEBI:CHEBI:143879"
FT /evidence="ECO:0000269|PubMed:15313614,
FT ECO:0007744|PDB:1XPY"
FT BINDING 195
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15313614,
FT ECO:0007744|PDB:1XPY, ECO:0007744|PDB:1XS2,
FT ECO:0007744|PDB:2GGH"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15313614,
FT ECO:0007744|PDB:1XPY, ECO:0007744|PDB:1XS2,
FT ECO:0007744|PDB:2GGH"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15313614"
FT BINDING 269
FT /ligand="N-acetyl-L-glutamine"
FT /ligand_id="ChEBI:CHEBI:143879"
FT /evidence="ECO:0000269|PubMed:15313614,
FT ECO:0007744|PDB:1XPY"
FT BINDING 299
FT /ligand="N-acetyl-L-glutamine"
FT /ligand_id="ChEBI:CHEBI:143879"
FT /evidence="ECO:0000269|PubMed:15313614,
FT ECO:0007744|PDB:1XPY"
FT MUTAGEN 48
FT /note="V->C: Loss of activity; when associated with C-120."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 56
FT /note="M->C: Loss of activity; when associated with C-65."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 60
FT /note="P->C: Loss of activity; when associated with C-100."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 65
FT /note="E->C: Loss of activity; when associated with C-56."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 68
FT /note="A->C: No change in activity; when associated with C-
FT 72."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 72
FT /note="D->C: No change in activity; when associated with C-
FT 68."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 100
FT /note="Y->C: Loss of activity; when associated with C-60."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 120
FT /note="R->C: Loss of activity; when associated with C-48."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 127
FT /note="G->C: Retains 93% of wild-type activity; when
FT associated with C-313."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 149
FT /note="E->C: Retains 88% of wild-type activity; when
FT associated with C-182."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 163
FT /note="G->C: Loss of activity; when associated with C-343."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 182
FT /note="A->C: Retains 88% of wild-type activity; when
FT associated with C-149."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 218
FT /note="Y->C: Retains 35% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 265
FT /note="V->C: Retains 39% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 313
FT /note="T->C: Retains 93% of wild-type activity; when
FT associated with C-127."
FT /evidence="ECO:0000269|PubMed:16650857"
FT MUTAGEN 343
FT /note="D->C: Loss of activity; when associated with C-163."
FT /evidence="ECO:0000269|PubMed:16650857"
FT STRAND 12..22
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2GGH"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2GGH"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:1R0M"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 104..122
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2GGH"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1XPY"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:1R0M"
FT TURN 270..274
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1R0M"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:1R0M"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:1R0M"
SQ SEQUENCE 375 AA; 40901 MW; 62F68CFA9FEF3DA4 CRC64;
MAHTGRMFKI EAAEIVVARL PLKFRFETSF GVQTHKVVPL LILHGEGVQG VAEGTMEARP
MYREETIAGA LDLLRGTFLP AILGQTFANP EAVADALGSY RGNRMARAMV EMAAWDLWAR
TLGVPLGTLL GGHKEQVEVG VSLGIQAGEQ ATVDLVRKHV EQGYRRIKLK IKPGWDVQPV
RATREAFPDI RLTVDANSAY TLADAGRLRQ LDEYDLTYIE QPLAWDDLVD HAELARRIRT
PLCLDESVAS AADARKALAL GAGGVINLKV ARVGGHAESR RVHDVAQSFG APVWCGGMLE
SGIGRAHNIH LSTLPNFRLP GDTSSASRYW ERDLIQEPLE AVDGLMPVPQ GPGTGVTLDR
EFLATVTEAQ EEHRA
