KAT1_HUMAN
ID KAT1_HUMAN Reviewed; 422 AA.
AC Q16773; Q5T275; Q8N191;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 1 {ECO:0000305|PubMed:19338303};
DE EC=2.6.1.7 {ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769};
DE AltName: Full=Cysteine-S-conjugate beta-lyase {ECO:0000305|PubMed:7883047};
DE EC=4.4.1.13 {ECO:0000269|PubMed:7883047};
DE AltName: Full=Glutamine transaminase K;
DE Short=GTK;
DE AltName: Full=Glutamine--phenylpyruvate transaminase {ECO:0000305|PubMed:7883047};
DE EC=2.6.1.64 {ECO:0000269|PubMed:7883047};
DE AltName: Full=Kynurenine aminotransferase 1 {ECO:0000312|HGNC:HGNC:1564};
DE AltName: Full=Kynurenine aminotransferase I;
DE Short=KATI;
DE AltName: Full=Kynurenine--oxoglutarate transaminase I;
GN Name=KYAT1 {ECO:0000312|HGNC:HGNC:1564}; Synonyms=CCBL1;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Kidney;
RX PubMed=7883047; DOI=10.1016/0014-5793(95)00123-q;
RA Perry S., Harries H., Scholfield C., Lock E., King L., Gibson G.,
RA Goldfarb P.;
RT "Molecular cloning and expression of a cDNA for human kidney cysteine
RT conjugate beta-lyase.";
RL FEBS Lett. 360:277-280(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0007744|PDB:1W7L, ECO:0007744|PDB:1W7M, ECO:0007744|PDB:1W7N}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND PHENYLALANINE, SUBUNIT, AND COFACTOR.
RX PubMed=15364907; DOI=10.1074/jbc.m409291200;
RA Rossi F., Han Q., Li J., Li J., Rizzi M.;
RT "Crystal structure of human kynurenine aminotransferase I.";
RL J. Biol. Chem. 279:50214-50220(2004).
RN [5] {ECO:0007744|PDB:3FVS, ECO:0007744|PDB:3FVU, ECO:0007744|PDB:3FVX}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH THE INHIBITORS
RP INDOLEACETIC ACID AND TRIS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PATHWAY, AND SUBUNIT.
RX PubMed=19338303; DOI=10.1021/jm9000874;
RA Han Q., Robinson H., Cai T., Tagle D.A., Li J.;
RT "Structural insight into the inhibition of human kynurenine
RT aminotransferase I/glutamine transaminase K.";
RL J. Med. Chem. 52:2786-2793(2009).
RN [6] {ECO:0007744|PDB:4WLH, ECO:0007744|PDB:4WLJ}
RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS)IN COMPLEX WITH INHIBITORS, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=28097769; DOI=10.1002/pro.3119;
RA Nadvi N.A., Salam N.K., Park J., Akladios F.N., Kapoor V., Collyer C.A.,
RA Gorrell M.D., Church W.B.;
RT "High resolution crystal structures of human kynurenine aminotransferase-I
RT bound to PLP cofactor, and in complex with aminooxyacetate.";
RL Protein Sci. 26:727-736(2017).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in
CC the tryptophan catabolic pathway which is also a broad spectrum
CC antagonist of the three ionotropic excitatory amino acid receptors
CC among others (PubMed:19338303, PubMed:28097769). Also metabolizes the
CC cysteine conjugates of certain halogenated alkenes and alkanes to form
CC reactive metabolites (PubMed:7883047). Catalyzes the beta-elimination
CC of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in
CC the cleavage of the C-S or C-Se bond (PubMed:7883047).
CC {ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769,
CC ECO:0000269|PubMed:7883047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7; Evidence={ECO:0000269|PubMed:19338303,
CC ECO:0000269|PubMed:28097769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000305|PubMed:19338303};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpyruvate + L-glutamine = 2-oxoglutaramate + L-
CC phenylalanine; Xref=Rhea:RHEA:17593, ChEBI:CHEBI:16769,
CC ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:58359; EC=2.6.1.64;
CC Evidence={ECO:0000269|PubMed:7883047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC Evidence={ECO:0000269|PubMed:7883047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000305|PubMed:7883047};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15364907};
CC -!- ACTIVITY REGULATION: Inhibited by tryptophan, indole-3-pyruvic acid, 3-
CC indolepropionic acid, DL-indole-3-lactic acid, indole-3-acetic acid
CC (IAC), amino-oxyacetate (AOAA), aminooxy-phenylpropionic acid (AOPP)
CC and Tris. {ECO:0000269|PubMed:19338303}.
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000269|PubMed:19338303,
CC ECO:0000269|PubMed:28097769}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15364907,
CC ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769}.
CC -!- INTERACTION:
CC Q16773; Q15645: TRIP13; NbExp=3; IntAct=EBI-10238309, EBI-358993;
CC Q16773; Q08AM6: VAC14; NbExp=4; IntAct=EBI-10238309, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7883047}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q16773-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16773-2; Sequence=VSP_009875;
CC Name=3;
CC IsoId=Q16773-3; Sequence=VSP_009876, VSP_009877;
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X82224; CAA57702.1; -; mRNA.
DR EMBL; AL441992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021262; AAH21262.1; -; mRNA.
DR EMBL; BC033685; AAH33685.1; -; mRNA.
DR CCDS; CCDS43884.1; -. [Q16773-1]
DR CCDS; CCDS48038.1; -. [Q16773-2]
DR PIR; S69001; S52790.
DR RefSeq; NP_001116143.1; NM_001122671.1. [Q16773-1]
DR RefSeq; NP_001116144.1; NM_001122672.1. [Q16773-2]
DR RefSeq; NP_004050.3; NM_004059.4. [Q16773-1]
DR RefSeq; XP_011517470.1; XM_011519168.1. [Q16773-1]
DR RefSeq; XP_011517471.1; XM_011519169.1. [Q16773-1]
DR RefSeq; XP_011517472.1; XM_011519170.2. [Q16773-1]
DR RefSeq; XP_016870754.1; XM_017015265.1. [Q16773-1]
DR RefSeq; XP_016870755.1; XM_017015266.1.
DR RefSeq; XP_016870756.1; XM_017015267.1. [Q16773-1]
DR RefSeq; XP_016870757.1; XM_017015268.1.
DR PDB; 1W7L; X-ray; 2.00 A; A=1-422.
DR PDB; 1W7M; X-ray; 2.70 A; A=1-422.
DR PDB; 1W7N; X-ray; 2.90 A; A=1-422.
DR PDB; 3FVS; X-ray; 1.50 A; A/B=1-422.
DR PDB; 3FVU; X-ray; 1.55 A; A/B=1-422.
DR PDB; 3FVX; X-ray; 1.50 A; A/B=1-422.
DR PDB; 4WLH; X-ray; 1.28 A; A/B=1-422.
DR PDB; 4WLJ; X-ray; 1.54 A; A/B=1-422.
DR PDB; 4WP0; X-ray; 3.00 A; A/B/C/D=1-422.
DR PDBsum; 1W7L; -.
DR PDBsum; 1W7M; -.
DR PDBsum; 1W7N; -.
DR PDBsum; 3FVS; -.
DR PDBsum; 3FVU; -.
DR PDBsum; 3FVX; -.
DR PDBsum; 4WLH; -.
DR PDBsum; 4WLJ; -.
DR PDBsum; 4WP0; -.
DR AlphaFoldDB; Q16773; -.
DR SMR; Q16773; -.
DR BioGRID; 107326; 17.
DR IntAct; Q16773; 7.
DR STRING; 9606.ENSP00000399415; -.
DR BindingDB; Q16773; -.
DR ChEMBL; CHEMBL3962; -.
DR DrugBank; DB02556; D-Phenylalanine.
DR DrugBank; DB07950; Indoleacetic acid.
DR DrugBank; DB00130; L-Glutamine.
DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR DrugBank; DB02142; Pyridoxamine-5'-Phosphate.
DR iPTMnet; Q16773; -.
DR PhosphoSitePlus; Q16773; -.
DR BioMuta; KYAT1; -.
DR DMDM; 46396284; -.
DR EPD; Q16773; -.
DR jPOST; Q16773; -.
DR MassIVE; Q16773; -.
DR MaxQB; Q16773; -.
DR PaxDb; Q16773; -.
DR PeptideAtlas; Q16773; -.
DR PRIDE; Q16773; -.
DR ProteomicsDB; 61059; -. [Q16773-1]
DR ProteomicsDB; 61060; -. [Q16773-2]
DR ProteomicsDB; 61061; -. [Q16773-3]
DR Antibodypedia; 7803; 242 antibodies from 28 providers.
DR DNASU; 883; -.
DR Ensembl; ENST00000302586.8; ENSP00000302227.3; ENSG00000171097.14. [Q16773-1]
DR Ensembl; ENST00000320665.10; ENSP00000317342.6; ENSG00000171097.14. [Q16773-2]
DR GeneID; 883; -.
DR KEGG; hsa:883; -.
DR MANE-Select; ENST00000302586.8; ENSP00000302227.3; NM_004059.5; NP_004050.3.
DR UCSC; uc004bwh.5; human. [Q16773-1]
DR CTD; 883; -.
DR DisGeNET; 883; -.
DR GeneCards; KYAT1; -.
DR HGNC; HGNC:1564; KYAT1.
DR HPA; ENSG00000171097; Low tissue specificity.
DR MIM; 600547; gene.
DR neXtProt; NX_Q16773; -.
DR OpenTargets; ENSG00000171097; -.
DR PharmGKB; PA26138; -.
DR VEuPathDB; HostDB:ENSG00000171097; -.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000158797; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; Q16773; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q16773; -.
DR TreeFam; TF105482; -.
DR BioCyc; MetaCyc:HS10240-MON; -.
DR BRENDA; 2.6.1.7; 2681.
DR PathwayCommons; Q16773; -.
DR Reactome; R-HSA-71240; Tryptophan catabolism.
DR Reactome; R-HSA-8964208; Phenylalanine metabolism.
DR Reactome; R-HSA-8964539; Glutamate and glutamine metabolism.
DR SignaLink; Q16773; -.
DR UniPathway; UPA00334; UER00726.
DR BioGRID-ORCS; 883; 15 hits in 1087 CRISPR screens.
DR ChiTaRS; KYAT1; human.
DR EvolutionaryTrace; Q16773; -.
DR GeneWiki; CCBL1; -.
DR GenomeRNAi; 883; -.
DR Pharos; Q16773; Tbio.
DR PRO; PR:Q16773; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q16773; protein.
DR Bgee; ENSG00000171097; Expressed in right hemisphere of cerebellum and 95 other tissues.
DR ExpressionAtlas; Q16773; baseline and differential.
DR Genevisible; Q16773; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IDA:FlyBase.
DR GO; GO:0047316; F:glutamine-phenylpyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006575; P:cellular modified amino acid metabolic process; IEA:InterPro.
DR GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR034614; KAT_I.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807:SF14; PTHR43807:SF14; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aminotransferase; Cytoplasm; Lyase;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..422
FT /note="Kynurenine--oxoglutarate transaminase 1"
FT /id="PRO_0000123942"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15364907,
FT ECO:0007744|PDB:1W7M"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15364907,
FT ECO:0007744|PDB:1W7M"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15364907,
FT ECO:0007744|PDB:1W7M"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:15364907,
FT ECO:0007744|PDB:1W7L, ECO:0007744|PDB:1W7M"
FT VAR_SEQ 68..117
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009875"
FT VAR_SEQ 230..250
FT /note="ASLPGMWERTLTIGSAGKTFS -> VSAAVLFGLGQPASLACGNGP (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009876"
FT VAR_SEQ 251..422
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009877"
FT CONFLICT 422
FT /note="L -> LWP (in Ref. 3; AAH33685)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3FVS"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1W7L"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:4WLJ"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 282..297
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 305..325
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:4WLH"
FT STRAND 335..343
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:4WLH"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:4WLJ"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:4WLH"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:4WLH"
SQ SEQUENCE 422 AA; 47875 MW; EAEF2F5E77A9B55A CRC64;
MAKQLQARRL DGIDYNPWVE FVKLASEHDV VNLGQGFPDF PPPDFAVEAF QHAVSGDFML
NQYTKTFGYP PLTKILASFF GELLGQEIDP LRNVLVTVGG YGALFTAFQA LVDEGDEVII
IEPFFDCYEP MTMMAGGRPV FVSLKPGPIQ NGELGSSSNW QLDPMELAGK FTSRTKALVL
NTPNNPLGKV FSREELELVA SLCQQHDVVC ITDEVYQWMV YDGHQHISIA SLPGMWERTL
TIGSAGKTFS ATGWKVGWVL GPDHIMKHLR TVHQNSVFHC PTQSQAAVAE SFEREQLLFR
QPSSYFVQFP QAMQRCRDHM IRSLQSVGLK PIIPQGSYFL ITDISDFKRK MPDLPGAVDE
PYDRRFVKWM IKNKGLVAIP VSIFYSVPHQ KHFDHYIRFC FVKDEATLQA MDEKLRKWKV
EL
