AAT_METJA
ID AAT_METJA Reviewed; 375 AA.
AC Q60317;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN OrderedLocusNames=MJ0001;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L77117; AAB97984.1; -; Genomic_DNA.
DR PIR; A64300; A64300.
DR RefSeq; WP_010869494.1; NC_000909.1.
DR AlphaFoldDB; Q60317; -.
DR SMR; Q60317; -.
DR STRING; 243232.MJ_0001; -.
DR EnsemblBacteria; AAB97984; AAB97984; MJ_0001.
DR GeneID; 1450840; -.
DR KEGG; mja:MJ_0001; -.
DR eggNOG; arCOG01130; Archaea.
DR HOGENOM; CLU_017584_4_3_2; -.
DR InParanoid; Q60317; -.
DR OMA; SVAMTGW; -.
DR OrthoDB; 32104at2157; -.
DR PhylomeDB; Q60317; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..375
FT /note="Probable aspartate aminotransferase"
FT /id="PRO_0000123858"
FT BINDING 31
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 223
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 42396 MW; 31349B11FC9B83A9 CRC64;
MISSRCKNIK PSAIREIFNL ATSDCINLGI GEPDFDTPKH IIEAAKRALD EGKTHYSPNN
GIPELREEIS NKLKDDYNLD VDKDNIIVTC GASEALMLSI MTLIDRGDEV LIPNPSFVSY
FSLTEFAEGK IKNIDLDENF NIDLEKVKES ITKKTKLIIF NSPSNPTGKV YDKETIKGLA
EIAEDYNLII VSDEVYDKII YDKKHYSPMQ FTDRCILING FSKTYAMTGW RIGYLAVSDE
LNKELDLINN MIKIHQYSFA CATTFAQYGA LAALRGSQKC VEDMVREFKM RRDLIYNGLK
DIFKVNKPDG AFYIFPDVSE YGDGVEVAKK LIENKVLCVP GVAFGENGAN YIRFSYATKY
EDIEKALGII KEIFE