ID B6K8B1_SCHJY Unreviewed; 424 AA. AC B6K8B1; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 11-JUL-2012, entry version 16. DE SubName: Full=Kynurenine-oxoglutarate transaminase; GN ORFNames=SJAG_04988; OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission OS yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; OC Schizosaccharomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OX NCBI_TaxID=402676; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=yFS275 / FY16936; RX PubMed=21511999; DOI=10.1126/science.1203357; RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., RA Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., RA Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., RA FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., RA Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., RA Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., RA Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., RA Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., RA Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.; RT "Comparative functional genomics of the fission yeasts."; RL Science 332:930-936(2011). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. 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; DS022230; EEB09765.1; -; Genomic_DNA. DR RefSeq; XP_002176058.1; XM_002176022.1. DR ProteinModelPortal; B6K8B1; -. DR GeneID; 7047471; -. DR OrthoDB; EOG4WHCV4; -. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Complete proteome; Pyridoxal phosphate. SQ SEQUENCE 424 AA; 47935 MW; D0C3BF7BFE8A7923 CRC64; MSGSKPALLP SARLAANRPD VWTFINQTAA QCKVPPVSLS QGFFNYNPPQ FILDAAKRAI DDVSCNQYQH TRGRLNLRKQ LSKTYSPLYN RELDPESQIL VTTGANEGFL SAFAAFLNPG DEVIVMEPFF DQYISNITMY GGVPVYVPII PPAAGSERPV SASEWKLDMQ RLRAAITSKT RMLVINTPHN PLGKVFSREE LLEIADVVLE NNLVVVSDEV YERLTYVDEF PRLATLRPEL FKHVIAVGSA GKTFGVTGWR IGWLIGDAHL IKYCSAAHTR ICFATNGPMQ QAIADSLAVA DQYNYFSEYV DSYKKRFRVL ADVFDELGLP YSQPEGTYYT MVNFSKVKVP EDYPVPDAIK DRPRDFKIAL WLMKEIGIAT IPPTEFFTDE DAHIADTYLR FAFCKTFDEL EEGARRLRKL KEYM //