THIC_ARATH
ID THIC_ARATH Reviewed; 644 AA.
AC O82392;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phosphomethylpyrimidine synthase, chloroplastic;
DE EC=4.1.99.17;
DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase;
DE Short=HMP-P synthase;
DE Short=HMP-phosphate synthase;
DE Short=HMPP synthase;
DE AltName: Full=Protein PYRIMIDINE REQUIRING;
DE AltName: Full=Thiamine biosynthesis protein ThiC;
DE Short=Protein THIAMINE C;
DE Flags: Precursor;
GN Name=THIC; Synonyms=PY; OrderedLocusNames=At2g29630; ORFNames=T27A16.27;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP REPRESSION BY THIAMINE VIA RIBOSWITCH REGULATION.
RX PubMed=16675665; DOI=10.1126/science.1128451;
RA Thore S., Leibundgut M., Ban N.;
RT "Structure of the eukaryotic thiamine pyrophosphate riboswitch with its
RT regulatory ligand.";
RL Science 312:1208-1211(2006).
RN [5]
RP REPRESSION BY THIAMINE VIA RIBOSWITCH REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=17993623; DOI=10.1105/tpc.107.053645;
RA Wachter A., Tunc-Ozdemir M., Grove B.C., Green P.J., Shintani D.K.,
RA Breaker R.R.;
RT "Riboswitch control of gene expression in plants by splicing and
RT alternative 3' end processing of mRNAs.";
RL Plant Cell 19:3437-3450(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, INDUCTION BY LIGHT, AND COFACTOR.
RC STRAIN=cv. Columbia;
RX PubMed=18048325; DOI=10.1073/pnas.0709597104;
RA Raschke M., Buerkle L., Mueller N., Nunes-Nesi A., Fernie A.R., Arigoni D.,
RA Amrhein N., Fitzpatrick T.B.;
RT "Vitamin B1 biosynthesis in plants requires the essential iron sulfur
RT cluster protein, THIC.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19637-19642(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=18332905; DOI=10.1038/cr.2008.35;
RA Kong D., Zhu Y., Wu H., Cheng X., Liang H., Ling H.-Q.;
RT "AtTHIC, a gene involved in thiamine biosynthesis in Arabidopsis
RT thaliana.";
RL Cell Res. 18:566-576(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [9]
RP INDUCTION BY ABSCISIC ACID; SALT AND OSMOTIC STRESS.
RX PubMed=22214485; DOI=10.1186/1471-2229-12-2;
RA Rapala-Kozik M., Wolak N., Kujda M., Banas A.K.;
RT "The upregulation of thiamine (vitamin B1) biosynthesis in Arabidopsis
RT thaliana seedlings under salt and osmotic stress conditions is mediated by
RT abscisic acid at the early stages of this stress response.";
RL BMC Plant Biol. 12:2-2(2012).
RN [10]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=23341335; DOI=10.1105/tpc.112.106385;
RA Bocobza S.E., Malitsky S., Araujo W.L., Nunes-Nesi A., Meir S., Shapira M.,
RA Fernie A.R., Aharoni A.;
RT "Orchestration of thiamin biosynthesis and central metabolism by combined
RT action of the thiamin pyrophosphate riboswitch and the circadian clock in
RT Arabidopsis.";
RL Plant Cell 25:288-307(2013).
RN [11]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=25014715; DOI=10.1042/bj20140522;
RA Zallot R., Yazdani M., Goyer A., Ziemak M.J., Guan J.C., McCarty D.R.,
RA de Crecy-Lagard V., Gerdes S., Garrett T.J., Benach J., Hunt J.F.,
RA Shintani D.K., Hanson A.D.;
RT "Salvage of the thiamin pyrimidine moiety by plant TenA proteins lacking an
RT active-site cysteine.";
RL Biochem. J. 463:145-155(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 72-644, AND SUBUNIT.
RX PubMed=24161603; DOI=10.1016/j.jsb.2013.10.005;
RA Coquille S., Roux C., Mehta A., Begley T.P., Fitzpatrick T.B., Thore S.;
RT "High-resolution crystal structure of the eukaryotic HMP-P synthase (THIC)
RT from Arabidopsis thaliana.";
RL J. Struct. Biol. 184:438-444(2013).
CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR)
CC in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
CC {ECO:0000269|PubMed:18048325, ECO:0000269|PubMed:18332905}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-
CC methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-
CC deoxyadenosine + CO + formate + 3 H(+) + L-methionine;
CC Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981;
CC EC=4.1.99.17;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:18048325, ECO:0000305|PubMed:24161603};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|PubMed:18048325};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24161603}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:18048325, ECO:0000269|PubMed:18332905,
CC ECO:0000269|PubMed:18431481}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in cotyledons, leaves, flowers
CC and siliques, and, to a lower extent, in roots (PubMed:18048325,
CC PubMed:25014715). Expressed in all green tissues, but not in roots,
CC seeds, and petals (PubMed:23341335). {ECO:0000269|PubMed:18048325,
CC ECO:0000269|PubMed:23341335, ECO:0000269|PubMed:25014715}.
CC -!- DEVELOPMENTAL STAGE: First detected in five-days seedlings. In
CC seedlings, mostly present at the root tips and in the jointed section
CC between the hypocotyl and root. In two-leaves seedlings, expressed in
CC leaves, cotyledons and vascular bundles of hypocotyls, and very weakly,
CC in the roots. In flowers, detected in sepals, filaments and pistil
CC tips, but not in petals. Later accumulates in the jointed region
CC between the silique and silique stem, and in the tips of siliques.
CC Decreasing expression during seed development (PubMed:25014715).
CC {ECO:0000269|PubMed:18048325, ECO:0000269|PubMed:18332905,
CC ECO:0000269|PubMed:25014715}.
CC -!- INDUCTION: Circadian-regulation (PubMed:23341335). Down-regulated by
CC extrinsic thiamine, via a vitamin B1 derivative thiamine pyrophosphate
CC (TPP)-sensing riboswitch regulation. Detected in both dark and light
CC grown seedlings; increased progressively after transfer of etiolated
CC seedlings to light. Up-regulated by salt, osmotic stress and abscisic
CC acid (PubMed:22214485). {ECO:0000269|PubMed:16675665,
CC ECO:0000269|PubMed:17993623, ECO:0000269|PubMed:18048325,
CC ECO:0000269|PubMed:18332905, ECO:0000269|PubMed:22214485,
CC ECO:0000269|PubMed:23341335}.
CC -!- DISRUPTION PHENOTYPE: Albino (white leaves) and lethal under normal
CC culture conditions, probably due to an impairment in thiamine
CC biosynthesis. {ECO:0000269|PubMed:18048325,
CC ECO:0000269|PubMed:18332905}.
CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000305}.
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DR EMBL; AC005496; AAC35232.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08281.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08282.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08283.1; -; Genomic_DNA.
DR EMBL; AY092989; AAM12988.1; -; mRNA.
DR EMBL; AY128756; AAM91156.1; -; mRNA.
DR PIR; F84698; F84698.
DR RefSeq; NP_001189634.1; NM_001202705.1.
DR RefSeq; NP_180524.1; NM_128517.4.
DR RefSeq; NP_850135.1; NM_179804.3.
DR PDB; 4N7Q; X-ray; 1.60 A; A=72-644.
DR PDB; 4S25; X-ray; 1.45 A; A=72-644.
DR PDB; 4S26; X-ray; 1.85 A; A/B=72-644.
DR PDB; 4S27; X-ray; 1.27 A; A=72-644.
DR PDB; 4S28; X-ray; 1.25 A; A=72-644.
DR PDB; 4S29; X-ray; 1.38 A; A=72-644.
DR PDBsum; 4N7Q; -.
DR PDBsum; 4S25; -.
DR PDBsum; 4S26; -.
DR PDBsum; 4S27; -.
DR PDBsum; 4S28; -.
DR PDBsum; 4S29; -.
DR AlphaFoldDB; O82392; -.
DR SMR; O82392; -.
DR BioGRID; 2863; 2.
DR STRING; 3702.AT2G29630.2; -.
DR iPTMnet; O82392; -.
DR PaxDb; O82392; -.
DR PRIDE; O82392; -.
DR ProteomicsDB; 246437; -.
DR EnsemblPlants; AT2G29630.1; AT2G29630.1; AT2G29630.
DR EnsemblPlants; AT2G29630.2; AT2G29630.2; AT2G29630.
DR EnsemblPlants; AT2G29630.3; AT2G29630.3; AT2G29630.
DR GeneID; 817513; -.
DR Gramene; AT2G29630.1; AT2G29630.1; AT2G29630.
DR Gramene; AT2G29630.2; AT2G29630.2; AT2G29630.
DR Gramene; AT2G29630.3; AT2G29630.3; AT2G29630.
DR KEGG; ath:AT2G29630; -.
DR Araport; AT2G29630; -.
DR TAIR; locus:2060604; AT2G29630.
DR eggNOG; ENOG502QRQ4; Eukaryota.
DR HOGENOM; CLU_013181_2_1_1; -.
DR InParanoid; O82392; -.
DR OrthoDB; 394937at2759; -.
DR PhylomeDB; O82392; -.
DR BioCyc; ARA:AT2G29630-MON; -.
DR BioCyc; MetaCyc:AT2G29630-MON; -.
DR BRENDA; 4.1.99.17; 399.
DR UniPathway; UPA00060; -.
DR PRO; PR:O82392; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82392; baseline and differential.
DR Genevisible; O82392; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0010266; P:response to vitamin B1; IEP:TAIR.
DR GO; GO:0009228; P:thiamine biosynthetic process; IMP:TAIR.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.540; -; 1.
DR HAMAP; MF_00089; ThiC; 1.
DR InterPro; IPR037509; ThiC.
DR InterPro; IPR038521; ThiC/Bza_core_dom.
DR InterPro; IPR002817; ThiC/BzaA/B.
DR PANTHER; PTHR30557; PTHR30557; 1.
DR Pfam; PF01964; ThiC_Rad_SAM; 1.
DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR TIGRFAMs; TIGR00190; thiC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Plastid; Reference proteome; S-adenosyl-L-methionine;
KW Thiamine biosynthesis; Transit peptide; Zinc.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 55..644
FT /note="Phosphomethylpyrimidine synthase, chloroplastic"
FT /id="PRO_0000415518"
FT REGION 55..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 342..344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 383..386
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:24161603"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 490
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:24161603"
FT BINDING 570
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 573
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT BINDING 578
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9A6Q5"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4N7Q"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 284..291
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 301..314
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 396..414
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 432..442
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 463..476
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 487..491
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 496..516
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 523..534
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 538..544
FT /evidence="ECO:0007829|PDB:4S28"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 562..566
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:4S28"
FT HELIX 579..590
FT /evidence="ECO:0007829|PDB:4S28"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:4S28"
SQ SEQUENCE 644 AA; 71987 MW; D1051F98A0200D21 CRC64;
MAASVHCTLM SVVCNNKNHS ARPKLPNSSL LPGFDVVVQA AATRFKKETT TTRATLTFDP
PTTNSERAKQ RKHTIDPSSP DFQPIPSFEE CFPKSTKEHK EVVHEESGHV LKVPFRRVHL
SGGEPAFDNY DTSGPQNVNA HIGLAKLRKE WIDRREKLGT PRYTQMYYAK QGIITEEMLY
CATREKLDPE FVRSEVARGR AIIPSNKKHL ELEPMIVGRK FLVKVNANIG NSAVASSIEE
EVYKVQWATM WGADTIMDLS TGRHIHETRE WILRNSAVPV GTVPIYQALE KVDGIAENLN
WEVFRETLIE QAEQGVDYFT IHAGVLLRYI PLTAKRLTGI VSRGGSIHAK WCLAYHKENF
AYEHWDDILD ICNQYDVALS IGDGLRPGSI YDANDTAQFA ELLTQGELTR RAWEKDVQVM
NEGPGHVPMH KIPENMQKQL EWCNEAPFYT LGPLTTDIAP GYDHITSAIG AANIGALGTA
LLCYVTPKEH LGLPNRDDVK AGVIAYKIAA HAADLAKQHP HAQAWDDALS KARFEFRWMD
QFALSLDPMT AMSFHDETLP ADGAKVAHFC SMCGPKFCSM KITEDIRKYA EENGYGSAEE
AIRQGMDAMS EEFNIAKKTI SGEQHGEVGG EIYLPESYVK AAQK
