ID KYNU_HUMAN Reviewed; 465 AA. AC Q16719; B2RCZ5; D3DP79; Q6I9T2; Q9BVW3; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 147. DE RecName: Full=Kynureninase {ECO:0000255|HAMAP-Rule:MF_03017}; DE EC=3.7.1.3 {ECO:0000255|HAMAP-Rule:MF_03017}; DE AltName: Full=L-kynurenine hydrolase {ECO:0000255|HAMAP-Rule:MF_03017}; GN Name=KYNU {ECO:0000255|HAMAP-Rule:MF_03017}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Hepatoma; RX PubMed=8706755; DOI=10.1111/j.1432-1033.1996.0460u.x; RA Alberati-Giani D., Buchli R., Malherbe P., Broger C., Lang G., RA Koehler C., Lahm H.-W., Cesura A.M.; RT "Isolation and expression of a cDNA clone encoding human RT kynureninase."; RL Eur. J. Biochem. 239:460-468(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC RP ACTIVITY, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Liver; RX PubMed=9180257; DOI=10.1016/S0014-5793(97)00374-8; RA Toma S., Nakamura M., Tone S., Okuno E., Kido R., Breton J., RA Avanzi N., Cozzi L., Speciale C., Mostardini M., Gatti S., Benatti L.; RT "Cloning and recombinant expression of rat and human kynureninase."; RL FEBS Lett. 408:5-10(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP GLU-412. RC TISSUE=Synovium; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP MASS SPECTROMETRY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=11985583; DOI=10.1046/j.1432-1033.2002.02854.x; RA Walsh H.A., Botting N.P.; RT "Purification and biochemical characterization of some of the RT properties of recombinant human kynureninase."; RL Eur. J. Biochem. 269:2069-2074(2002). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL RP PHOSPHATE, HOMODIMERIZATION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17300176; DOI=10.1021/bi0616697; RA Lima S., Khristoforov R., Momany C., Phillips R.S.; RT "Crystal structure of Homo sapiens kynureninase."; RL Biochemistry 46:2735-2744(2007). RN [13] RP INVOLVEMENT IN HYXKY, AND VARIANT HYXKY ALA-198. RX PubMed=17334708; DOI=10.1007/s10545-007-0396-2; RA Christensen M., Duno M., Lund A.M., Skovby F., Christensen E.; RT "Xanthurenic aciduria due to a mutation in KYNU encoding RT kynureninase."; RL J. Inherit. Metab. Dis. 30:248-255(2007). CC -!- FUNCTION: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- CC hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- CC hydroxyanthranilic acid (3-OHAA), respectively. Has a preference CC for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase CC activity. CC -!- CATALYTIC ACTIVITY: L-kynurenine + H(2)O = anthranilate + L- CC alanine. {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- CATALYTIC ACTIVITY: L-3-hydroxykynurenine + H(2)O = 3- CC hydroxyanthranilate + L-alanine. {ECO:0000255|HAMAP- CC Rule:MF_03017}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- ENZYME REGULATION: Inhibited by o-methoxybenzoylalanine (OMBA). CC {ECO:0000269|PubMed:8706755, ECO:0000269|PubMed:9180257}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=493 uM for L-kynurenine (at pH 7.0) CC {ECO:0000269|PubMed:11985583, ECO:0000269|PubMed:17300176, CC ECO:0000269|PubMed:8706755, ECO:0000269|PubMed:9180257}; CC KM=28.3 uM for DL-3-hydroxykynurenine (at pH 7.0) CC {ECO:0000269|PubMed:11985583, ECO:0000269|PubMed:17300176, CC ECO:0000269|PubMed:8706755, ECO:0000269|PubMed:9180257}; CC KM=3.0 uM for DL-3-hydroxykynurenine (at pH 7.9) CC {ECO:0000269|PubMed:11985583, ECO:0000269|PubMed:17300176, CC ECO:0000269|PubMed:8706755, ECO:0000269|PubMed:9180257}; CC pH dependence: CC Optimum pH is 8.25 with DL-3-hydroxykynurenine as substrate. CC {ECO:0000269|PubMed:11985583, ECO:0000269|PubMed:17300176, CC ECO:0000269|PubMed:8706755, ECO:0000269|PubMed:9180257}; CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; L- CC alanine and anthranilate from L-kynurenine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from L-kynurenine: step 2/3. {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03017, CC ECO:0000269|PubMed:17300176}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03017, CC ECO:0000269|PubMed:8706755}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q16719-1; Sequence=Displayed; CC Name=2; CC IsoId=Q16719-2; Sequence=VSP_042739, VSP_042740; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested (heart, brain CC placenta, lung, liver, skeletal muscle, kidney and pancreas). CC Highest levels found in placenta, liver and lung. Expressed in all CC brain regions. {ECO:0000269|PubMed:8706755, CC ECO:0000269|PubMed:9180257}. CC -!- INDUCTION: Increased levels in several cerebral and systemic CC inflammatory conditions. CC -!- MASS SPECTROMETRY: Mass=52400; Method=MALDI; Range=1-465; Note=The CC reported mass is given to only three significant figures.; CC Evidence={ECO:0000269|PubMed:11985583}; CC -!- DISEASE: Hydroxykynureninuria (HYXKY) [MIM:236800]: An inborn CC error of amino acid metabolism characterized by massive urinary CC excretion of large amounts of kynurenine, 3-hydroxykynurenine and CC xanthurenic acid. Affected individuals manifest renal tubular CC dysfunction, metabolic acidosis, psychomotor retardation, non- CC progressive encephalopathy, and muscular hypertonia. CC {ECO:0000269|PubMed:17334708}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the kynureninase family. CC {ECO:0000255|HAMAP-Rule:MF_03017}. CC -!- CAUTION: It has been reported that this enzyme possesses no CC measurable activity against L-kynurenine and is subject to CC inhibition by both L-kynurenine and D-kynurenine at pH 7.9. CC {ECO:0000305|PubMed:11985583}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U57721; AAC50650.1; -; mRNA. DR EMBL; AK315343; BAG37742.1; -; mRNA. DR EMBL; CR457423; CAG33704.1; -; mRNA. DR EMBL; AC013437; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC013444; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471058; EAX11599.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11600.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11601.1; -; Genomic_DNA. DR EMBL; BC000879; AAH00879.1; -; mRNA. DR CCDS; CCDS2183.1; -. [Q16719-1] DR CCDS; CCDS33299.1; -. [Q16719-2] DR PIR; G02652; G02652. DR RefSeq; NP_001028170.1; NM_001032998.1. [Q16719-2] DR RefSeq; NP_001186170.1; NM_001199241.1. [Q16719-1] DR RefSeq; NP_003928.1; NM_003937.2. [Q16719-1] DR RefSeq; XP_011510403.1; XM_011512101.1. [Q16719-1] DR UniGene; Hs.470126; -. DR PDB; 2HZP; X-ray; 2.00 A; A=1-465. DR PDB; 3E9K; X-ray; 1.70 A; A=1-465. DR PDBsum; 2HZP; -. DR PDBsum; 3E9K; -. DR ProteinModelPortal; Q16719; -. DR SMR; Q16719; 6-460. DR BioGrid; 114454; 31. DR IntAct; Q16719; 1. DR STRING; 9606.ENSP00000264170; -. DR BindingDB; Q16719; -. DR ChEMBL; CHEMBL5100; -. DR DrugBank; DB00160; L-Alanine. DR PhosphoSite; Q16719; -. DR BioMuta; KYNU; -. DR DMDM; 3913982; -. DR MaxQB; Q16719; -. DR PaxDb; Q16719; -. DR PeptideAtlas; Q16719; -. DR PRIDE; Q16719; -. DR DNASU; 8942; -. DR Ensembl; ENST00000264170; ENSP00000264170; ENSG00000115919. [Q16719-1] DR Ensembl; ENST00000375773; ENSP00000364928; ENSG00000115919. [Q16719-2] DR Ensembl; ENST00000409512; ENSP00000386731; ENSG00000115919. [Q16719-1] DR GeneID; 8942; -. DR KEGG; hsa:8942; -. DR UCSC; uc002tvk.3; human. [Q16719-2] DR UCSC; uc002tvl.3; human. [Q16719-1] DR CTD; 8942; -. DR GeneCards; KYNU; -. DR HGNC; HGNC:6469; KYNU. DR HPA; HPA031686; -. DR MIM; 236800; phenotype. DR MIM; 605197; gene. DR neXtProt; NX_Q16719; -. DR Orphanet; 79155; Encephalopathy due to hydroxykynureninuria. DR PharmGKB; PA30258; -. DR eggNOG; KOG3846; Eukaryota. DR eggNOG; COG3844; LUCA. DR GeneTree; ENSGT00390000008033; -. DR HOGENOM; HOG000242438; -. DR HOVERGEN; HBG001170; -. DR InParanoid; Q16719; -. DR KO; K01556; -. DR OMA; TWSSIGV; -. DR OrthoDB; EOG7D2FDV; -. DR PhylomeDB; Q16719; -. DR TreeFam; TF300707; -. DR BioCyc; MetaCyc:HS03952-MONOMER; -. DR BRENDA; 3.7.1.3; 2681. DR Reactome; R-HSA-71240; Tryptophan catabolism. DR UniPathway; UPA00253; UER00329. DR UniPathway; UPA00334; UER00455. DR ChiTaRS; KYNU; human. DR EvolutionaryTrace; Q16719; -. DR GeneWiki; Kynureninase; -. DR GenomeRNAi; 8942; -. DR NextBio; 33630; -. DR PRO; PR:Q16719; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; Q16719; -. DR CleanEx; HS_KYNU; -. DR ExpressionAtlas; Q16719; baseline and differential. DR Genevisible; Q16719; HS. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0030429; F:kynureninase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0034354; P:'de novo' NAD biosynthetic process from tryptophan; IEA:UniProtKB-HAMAP. DR GO; GO:0043420; P:anthranilate metabolic process; IDA:UniProtKB. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019805; P:quinolinate biosynthetic process; IDA:UniProtKB. DR GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB. DR GO; GO:0034516; P:response to vitamin B6; IMP:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006569; P:tryptophan catabolic process; IMP:UniProtKB. DR GO; GO:0019442; P:tryptophan catabolic process to acetyl-CoA; IEA:Ensembl. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:Ensembl. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01970; Kynureninase; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR010111; Kynureninase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR14084; PTHR14084; 1. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF038800; KYNU; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01814; kynureninase; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; Disease mutation; Hydrolase; Polymorphism; KW Pyridine nucleotide biosynthesis; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 465 Kynureninase. FT /FTId=PRO_0000218657. FT REGION 165 168 Pyridoxal phosphate binding. FT BINDING 137 137 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_03017}. FT BINDING 138 138 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017, FT ECO:0000269|PubMed:17300176}. FT BINDING 221 221 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017}. FT BINDING 250 250 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017, FT ECO:0000269|PubMed:17300176}. FT BINDING 253 253 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017, FT ECO:0000269|PubMed:17300176}. FT BINDING 275 275 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017, FT ECO:0000269|PubMed:17300176}. FT BINDING 305 305 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017, FT ECO:0000269|PubMed:17300176}. FT BINDING 333 333 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_03017, FT ECO:0000269|PubMed:17300176}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000244|PubMed:22814378}. FT MOD_RES 276 276 N6-(pyridoxal phosphate)lysine. FT VAR_SEQ 302 307 LVGWFG -> RSEFFN (in isoform 2). FT {ECO:0000305}. FT /FTId=VSP_042739. FT VAR_SEQ 308 465 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_042740. FT VARIANT 188 188 R -> Q (in dbSNP:rs2304705). FT /FTId=VAR_049724. FT VARIANT 198 198 T -> A (in HYXKY). FT {ECO:0000269|PubMed:17334708}. FT /FTId=VAR_054401. FT VARIANT 412 412 K -> E (in dbSNP:rs9013). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_022092. FT HELIX 9 20 {ECO:0000244|PDB:3E9K}. FT HELIX 27 35 {ECO:0000244|PDB:3E9K}. FT HELIX 40 45 {ECO:0000244|PDB:3E9K}. FT HELIX 51 53 {ECO:0000244|PDB:3E9K}. FT HELIX 59 61 {ECO:0000244|PDB:3E9K}. FT TURN 73 75 {ECO:0000244|PDB:3E9K}. FT HELIX 83 97 {ECO:0000244|PDB:3E9K}. FT HELIX 98 102 {ECO:0000244|PDB:3E9K}. FT STRAND 104 107 {ECO:0000244|PDB:3E9K}. FT HELIX 109 111 {ECO:0000244|PDB:3E9K}. FT HELIX 114 117 {ECO:0000244|PDB:3E9K}. FT HELIX 118 120 {ECO:0000244|PDB:3E9K}. FT HELIX 121 124 {ECO:0000244|PDB:3E9K}. FT HELIX 128 130 {ECO:0000244|PDB:3E9K}. FT STRAND 131 133 {ECO:0000244|PDB:3E9K}. FT HELIX 137 148 {ECO:0000244|PDB:3E9K}. FT STRAND 153 155 {ECO:0000244|PDB:3E9K}. FT STRAND 157 161 {ECO:0000244|PDB:3E9K}. FT HELIX 166 178 {ECO:0000244|PDB:3E9K}. FT HELIX 183 186 {ECO:0000244|PDB:3E9K}. FT STRAND 187 190 {ECO:0000244|PDB:3E9K}. FT HELIX 201 211 {ECO:0000244|PDB:3E9K}. FT HELIX 212 214 {ECO:0000244|PDB:3E9K}. FT STRAND 215 223 {ECO:0000244|PDB:3E9K}. FT TURN 225 227 {ECO:0000244|PDB:3E9K}. FT HELIX 233 242 {ECO:0000244|PDB:3E9K}. FT STRAND 246 250 {ECO:0000244|PDB:3E9K}. FT TURN 252 257 {ECO:0000244|PDB:3E9K}. FT HELIX 262 265 {ECO:0000244|PDB:3E9K}. FT STRAND 269 272 {ECO:0000244|PDB:3E9K}. FT STRAND 274 276 {ECO:0000244|PDB:3E9K}. FT STRAND 287 290 {ECO:0000244|PDB:3E9K}. FT HELIX 292 294 {ECO:0000244|PDB:3E9K}. FT TURN 295 297 {ECO:0000244|PDB:3E9K}. FT HELIX 305 307 {ECO:0000244|PDB:3E9K}. FT HELIX 310 313 {ECO:0000244|PDB:3E9K}. FT HELIX 326 329 {ECO:0000244|PDB:3E9K}. FT HELIX 336 352 {ECO:0000244|PDB:3E9K}. FT HELIX 354 375 {ECO:0000244|PDB:3E9K}. FT STRAND 388 390 {ECO:0000244|PDB:3E9K}. FT HELIX 396 398 {ECO:0000244|PDB:3E9K}. FT STRAND 403 407 {ECO:0000244|PDB:3E9K}. FT HELIX 414 419 {ECO:0000244|PDB:3E9K}. FT TURN 420 422 {ECO:0000244|PDB:3E9K}. FT STRAND 426 428 {ECO:0000244|PDB:3E9K}. FT TURN 429 431 {ECO:0000244|PDB:3E9K}. FT STRAND 432 436 {ECO:0000244|PDB:3E9K}. FT TURN 439 441 {ECO:0000244|PDB:3E9K}. FT HELIX 444 458 {ECO:0000244|PDB:3E9K}. SQ SEQUENCE 465 AA; 52352 MW; BDD136BE18C79EBB CRC64; MEPSSLELPA DTVQRIAAEL KCHPTDERVA LHLDEEDKLR HFRECFYIPK IQDLPPVDLS LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIAAY GHEVGKRPWI TGDESIVGLM KDIVGANEKE IALMNALTVN LHLLMLSFFK PTPKRYKILL EAKAFPSDHY AIESQLQLHG LNIEESMRMI KPREGEETLR IEDILEVIEK EGDSIAVILF SGVHFYTGQH FNIPAITKAG QAKGCYVGFD LAHAVGNVEL YLHDWGVDFA CWCSYKYLNA GAGGIAGAFI HEKHAHTIKP ALVGWFGHEL STRFKMDNKL QLIPGVCGFR ISNPPILLVC SLHASLEIFK QATMKALRKK SVLLTGYLEY LIKHNYGKDK AATKKPVVNI ITPSHVEERG CQLTITFSVP NKDVFQELEK RGVVCDKRNP NGIRVAPVPL YNSFHDVYKF TNLLTSILDS AETKN //