ID   SDHL_HUMAN              Reviewed;         328 AA.
AC   P20132; A8K9P5;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   02-SEP-2026, entry version 208.
DE   RecName: Full=L-serine dehydratase/L-threonine deaminase;
DE            Short=SDH;
DE            EC=4.3.1.17 {ECO:0000269|PubMed:15618015, ECO:0000269|PubMed:15689518, ECO:0000269|PubMed:16580895, ECO:0000269|PubMed:18342636};
DE   AltName: Full=Hepatic serine dehydratase {ECO:0000303|PubMed:16580895};
DE            Short=hSDH {ECO:0000303|PubMed:16580895};
DE   AltName: Full=L-serine deaminase;
DE   AltName: Full=L-threonine dehydratase;
DE            Short=TDH;
DE            EC=4.3.1.19 {ECO:0000269|PubMed:16580895, ECO:0000269|PubMed:18342636};
GN   Name=SDS; Synonyms=SDH;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=2674117; DOI=10.1016/s0021-9258(18)71550-0;
RA   Ogawa H., Gomi T., Konishi K., Date T., Nakashima H., Nose K., Matsuda Y.,
RA   Peraino C., Pitot H.C., Fujioka M.;
RT   "Human liver serine dehydratase. cDNA cloning and sequence homology with
RT   hydroxyamino acid dehydratases from other sources.";
RL   J. Biol. Chem. 264:15818-15823(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 1-10, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15618015; DOI=10.1016/j.biocel.2004.08.004;
RA   Kashii T., Gomi T., Oya T., Ishii Y., Oda H., Maruyama M., Kobayashi M.,
RA   Masuda T., Yamazaki M., Nagata T., Tsukada K., Nakajima A., Tatsu K.,
RA   Mori H., Takusagawa F., Ogawa H., Pitot H.C.;
RT   "Some biochemical and histochemical properties of human liver serine
RT   dehydratase.";
RL   Int. J. Biochem. Cell Biol. 37:574-589(2005).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   SUBUNIT, BINDING, AND MUTAGENESIS OF PRO-128.
RX   PubMed=16580895; DOI=10.1016/j.bbapap.2006.02.010;
RA   Ogawa H., Gomi T., Nishizawa M., Hayakawa Y., Endo S., Hayashi K.,
RA   Ochiai H., Takusagawa F., Pitot H.C., Mori H., Sakurai H., Koizumi K.,
RA   Saiki I., Oda H., Fujishita T., Miwa T., Maruyama M., Kobayashi M.;
RT   "Enzymatic and biochemical properties of a novel human serine dehydratase
RT   isoform.";
RL   Biochim. Biophys. Acta 1764:961-971(2006).
RN   [6]
RP   CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-303, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND FUNCTION.
RX   PubMed=18342636; DOI=10.1016/j.bbagen.2008.01.020;
RA   Yamada T., Komoto J., Kasuya T., Takata Y., Ogawa H., Mori H.,
RA   Takusagawa F.;
RT   "A catalytic mechanism that explains a low catalytic activity of serine
RT   dehydratase like-1 from human cancer cells: crystal structure and site-
RT   directed mutagenesis studies.";
RL   Biochim. Biophys. Acta 1780:809-818(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP   AND SUBUNIT.
RX   PubMed=14646100; DOI=10.1107/s0907444903020110;
RA   Sun L., Li X., Dong Y., Yang M., Liu Y., Han X., Zhang X., Pang H., Rao Z.;
RT   "Crystallization and preliminary crystallographic analysis of human serine
RT   dehydratase.";
RL   Acta Crystallogr. D 59:2297-2299(2003).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RX   PubMed=15689518; DOI=10.1110/ps.041179105;
RA   Sun L., Bartlam M., Liu Y., Pang H., Rao Z.;
RT   "Crystal structure of the pyridoxal-5'-phosphate-dependent serine
RT   dehydratase from human liver.";
RL   Protein Sci. 14:791-798(2005).
CC   -!- FUNCTION: Catalyzes the pyridoxal-phosphate-dependent dehydrative
CC       deamination of L-threonine and L-serine to ammonia and alpha-
CC       ketobutyrate and pyruvate, respectively. {ECO:0000269|PubMed:15618015,
CC       ECO:0000269|PubMed:15689518, ECO:0000269|PubMed:16580895,
CC       ECO:0000269|PubMed:18342636}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine = pyruvate + NH4(+); Xref=Rhea:RHEA:19169,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC         Evidence={ECO:0000269|PubMed:15618015, ECO:0000269|PubMed:15689518,
CC         ECO:0000269|PubMed:16580895, ECO:0000269|PubMed:18342636};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC         Evidence={ECO:0000269|PubMed:16580895, ECO:0000269|PubMed:18342636};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:15689518, ECO:0000269|PubMed:16580895};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23 mM for L-serine {ECO:0000269|PubMed:18342636};
CC         KM=67.3 mM for L-serine {ECO:0000269|PubMed:16580895};
CC         KM=50 mM for L-serine {ECO:0000269|PubMed:15618015};
CC         KM=31 mM for L-threonine {ECO:0000269|PubMed:18342636};
CC         KM=59.5 mM for L-threonine {ECO:0000269|PubMed:16580895};
CC         KM=57 mM for L-threonine {ECO:0000269|PubMed:15618015};
CC         Vmax=105.6 nmol/min/mg enzyme for L-serine
CC         {ECO:0000269|PubMed:16580895};
CC         Vmax=137 nmol/min/mg enzyme for L-serine
CC         {ECO:0000269|PubMed:15618015};
CC         Vmax=70.6 nmol/min/mg enzyme for L-threonine
CC         {ECO:0000269|PubMed:16580895};
CC         Vmax=96 nmol/min/mg enzyme for L-threonine
CC         {ECO:0000269|PubMed:15618015};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14646100,
CC       ECO:0000269|PubMed:15618015, ECO:0000269|PubMed:15689518,
CC       ECO:0000269|PubMed:16580895}.
CC   -!- INTERACTION:
CC       P20132; Q8WTU0: DDI1; NbExp=3; IntAct=EBI-17859611, EBI-748248;
CC       P20132; O14964: HGS; NbExp=3; IntAct=EBI-17859611, EBI-740220;
CC       P20132; Q96PF1: TGM7; NbExp=3; IntAct=EBI-17859611, EBI-12029034;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P09367}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the perivenous regions
CC       of the liver. {ECO:0000269|PubMed:15618015}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000305}.
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DR   EMBL; J05037; AAA36604.1; -; mRNA.
DR   EMBL; AK292760; BAF85449.1; -; mRNA.
DR   EMBL; CH471054; EAW98054.1; -; Genomic_DNA.
DR   CCDS; CCDS9169.1; -.
DR   PIR; A34232; DWHUT.
DR   RefSeq; NP_006834.2; NM_006843.3.
DR   PDB; 1P5J; X-ray; 2.50 A; A=1-328.
DR   PDB; 4H27; X-ray; 1.30 A; A=1-328.
DR   AlphaFoldDB; P20132; -.
DR   SMR; P20132; -.
DR   BioGRID; 116189; 8.
DR   FunCoup; P20132; 626.
DR   IntAct; P20132; 4.
DR   NDEx; IQUERY-CP-SDS; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000257549; -.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   DrugBank; DB00133; Serine.
DR   iPTMnet; P20132; -.
DR   PhosphoSitePlus; P20132; -.
DR   BioMuta; SDS; -.
DR   DMDM; 229462819; -.
DR   MassIVE; P20132; -.
DR   PaxDb; 9606-ENSP00000257549; -.
DR   PeptideAtlas; P20132; -.
DR   ProteomicsDB; 53724; -.
DR   Antibodypedia; 31269; 270 antibodies from 19 providers.
DR   DNASU; 10993; -.
DR   Ensembl; ENST00000257549.9; ENSP00000257549.4; ENSG00000135094.12.
DR   Ensembl; ENST00000880846.1; ENSP00000550905.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880847.1; ENSP00000550906.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880848.1; ENSP00000550907.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880849.1; ENSP00000550908.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880851.1; ENSP00000550910.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880852.1; ENSP00000550911.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880853.1; ENSP00000550912.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880854.1; ENSP00000550913.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880855.1; ENSP00000550914.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880857.1; ENSP00000550916.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880858.1; ENSP00000550917.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880863.1; ENSP00000550922.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880864.1; ENSP00000550923.1; ENSG00000135094.12.
DR   Ensembl; ENST00000880865.1; ENSP00000550924.1; ENSG00000135094.12.
DR   GeneID; 10993; -.
DR   KEGG; hsa:10993; -.
DR   MANE-Select; ENST00000257549.9; ENSP00000257549.4; NM_006843.3; NP_006834.2.
DR   UCSC; uc001tvg.4; human.
DR   AGR; HGNC:10691; -.
DR   ClinPGx; PA35616; -.
DR   CTD; 10993; -.
DR   DisGeNET; 10993; -.
DR   GeneCards; SDS; -.
DR   HGNC; HGNC:10691; SDS.
DR   HPA; ENSG00000135094; Tissue enriched (liver).
DR   MIM; 182128; gene.
DR   OpenTargets; ENSG00000135094; -.
DR   VEuPathDB; HostDB:ENSG00000135094; -.
DR   eggNOG; KOG1250; Eukaryota.
DR   GeneTree; ENSGT00940000160172; -.
DR   HOGENOM; CLU_021152_3_0_1; -.
DR   InParanoid; P20132; -.
DR   OMA; AEQGCEH; -.
DR   OrthoDB; 7773036at2759; -.
DR   PAN-GO; P20132; 4 GO annotations based on evolutionary models.
DR   PhylomeDB; P20132; -.
DR   BioCyc; MetaCyc:HS05952-MONOMER; -.
DR   BRENDA; 4.3.1.17; 2681.
DR   PathwayCommons; P20132; -.
DR   Reactome; R-HSA-8849175; Threonine catabolism.
DR   Reactome; R-HSA-977347; Serine metabolism.
DR   SABIO-RK; P20132; -.
DR   SignaLink; P20132; -.
DR   UniPathway; UPA00138; -.
DR   Agora; ENSG00000135094; -.
DR   BioGRID-ORCS; 10993; 14 hits in 1158 CRISPR screens.
DR   ChiTaRS; SDS; human.
DR   EvolutionaryTrace; P20132; -.
DR   GenomeRNAi; 10993; -.
DR   Pharos; P20132; Tbio.
DR   PRO; PR:P20132; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P20132; protein.
DR   Bgee; ENSG00000135094; Expressed in right lobe of liver and 108 other cell types or tissues.
DR   ExpressionAtlas; P20132; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:0004794; F:threonine deaminase activity; IDA:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006565; P:L-serine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006567; P:L-threonine catabolic process; IBA:GO_Central.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; IDA:UniProtKB.
DR   CDD; cd06448; L-Ser-dehyd; 1.
DR   FunFam; 3.40.50.1100:FF:000031; L-serine dehydratase/L-threonine deaminase; 1.
DR   FunFam; 3.40.50.1100:FF:000106; L-serine dehydratase/L-threonine deaminase; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR050147; Ser/Thr_Dehydratase.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR48078:SF8; L-SERINE DEHYDRATASE_L-THREONINE DEAMINASE; 1.
DR   PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
DR   PDBsum; 1P5J; -.
DR   PDBsum; 4H27; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW   Lipid metabolism; Lyase; Proteomics identification; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..328
FT                   /note="L-serine dehydratase/L-threonine deaminase"
FT                   /id="PRO_0000185594"
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:16580895"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:15689518"
FT   MUTAGEN         128
FT                   /note="Missing: Reduced Km and Vmax for both L-serine and
FT                   L-threonine. 10-fold increase in dissociation constant for
FT                   pyridoxal-phosphate."
FT                   /evidence="ECO:0000269|PubMed:16580895"
FT   MUTAGEN         303
FT                   /note="C->A: Loss of enzyme activity."
FT                   /evidence="ECO:0000269|PubMed:18342636"
FT   CONFLICT        89
FT                   /note="S -> G (in Ref. 1; AAA36604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="V -> C (in Ref. 1; AAA36604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="V -> C (in Ref. 1; AAA36604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        230
FT                   /note="A -> S (in Ref. 1; AAA36604)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="C -> W (in Ref. 1; AAA36604)"
FT                   /evidence="ECO:0000305"
FT   STRAND          13..16
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           17..23
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          25..31
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1P5J"
FT   HELIX           41..54
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           93..100
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           115..126
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          130..133
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           139..145
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           147..155
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          161..166
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           171..182
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          190..195
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           200..207
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           221..223
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           230..236
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           248..262
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           268..278
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           281..287
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   STRAND          297..302
FT                   /evidence="ECO:0007829|PDB:4H27"
FT   HELIX           310..319
FT                   /evidence="ECO:0007829|PDB:4H27"
SQ   SEQUENCE   328 AA;  34625 MW;  F6E9AB01D6308C83 CRC64;
     MMSGEPLHVK TPIRDSMALS KMAGTSVYLK MDSAQPSGSF KIRGIGHFCK RWAKQGCAHF
     VCSSAGNAGM AAAYAARQLG VPATIVVPST TPALTIERLK NEGATVKVVG ELLDEAFELA
     KALAKNNPGW VYIPPFDDPL IWEGHASIVK ELKETLWEKP GAIALSVGGG GLLCGVVQGL
     QEVGWGDVPV IAMETFGAHS FHAATTAGKL VSLPKITSVA KALGVKTVGA QALKLFQEHP
     IFSEVISDQE AVAAIEKFVD DEKILVEPAC GAALAAVYSH VIQKLQLEGN LRTPLPSLVV
     IVCGGSNISL AQLRALKEQL GMTNRLPK
//