ID   Y1479_METJA             Reviewed;         432 AA.
AC   Q58874;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Uncharacterized aminotransferase MJ1479;
DE            EC=2.6.1.-;
GN   OrderedLocusNames=MJ1479;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L77117; AAB99491.1; -; Genomic_DNA.
DR   PIR; F64484; F64484.
DR   RefSeq; WP_010871000.1; NC_000909.1.
DR   AlphaFoldDB; Q58874; -.
DR   SMR; Q58874; -.
DR   STRING; 243232.MJ_1479; -.
DR   EnsemblBacteria; AAB99491; AAB99491; MJ_1479.
DR   GeneID; 1452384; -.
DR   KEGG; mja:MJ_1479; -.
DR   eggNOG; arCOG01135; Archaea.
DR   HOGENOM; CLU_017584_4_2_2; -.
DR   InParanoid; Q58874; -.
DR   OMA; FGFECPP; -.
DR   OrthoDB; 32104at2157; -.
DR   PhylomeDB; Q58874; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..432
FT                   /note="Uncharacterized aminotransferase MJ1479"
FT                   /id="PRO_0000163832"
FT   MOD_RES         243
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   432 AA;  49430 MW;  14D1602E32DB31FE CRC64;
     MRNPIIDVGA KELSYEIREI VDVAKKIEEF GINITWENIG DPVAKGEKIP DWIKDIIAEI
     VKNDCSYAYC PTKGLLETRE FLAEQVNKRG GVQITAEDII FFNGLGDAIA KIYGLLKRQV
     RVINPSPSYS THSSAEASHA GSPPVTYFLD PYNYWYPDID DLEKRIKYNP AVSGILVINP
     DNPTGAVYPK KILNEIVDLA NEYDLFIICD EIYCNLVYNG KKQHLLCEVI DDVCGLSLKG
     ISKELPWPGA RCGWIEIYNA DKDEEFKKYV ESIYKAKLIE VCSTTLPQMA IPRIMGHRNY
     KKYLEERNRF FEKRSNTAYK KLKDLDGVIA NKANGAFYMS VVFEDNYLNG NNSIKIENEK
     LKEFIEHQIK DASIDKKFVY YLLASTGICV VPLTSFCSQL NGFRVTLLER DDEKFEWIFD
     TLAEKIDEFL KT