ID   B1L3P7_KORCO            Unreviewed;       359 AA.
AC   B1L3P7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Aspartate/tyrosine/aromatic aminotransferase {ECO:0000313|EMBL:ACB07076.1};
GN   OrderedLocusNames=Kcr_0318 {ECO:0000313|EMBL:ACB07076.1};
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Korarchaeum.
OX   NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB07076.1, ECO:0000313|Proteomes:UP000001686};
RN   [1] {ECO:0000313|EMBL:ACB07076.1, ECO:0000313|Proteomes:UP000001686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CP000968; ACB07076.1; -; Genomic_DNA.
DR   RefSeq; WP_012308973.1; NC_010482.1.
DR   AlphaFoldDB; B1L3P7; -.
DR   STRING; 374847.Kcr_0318; -.
DR   EnsemblBacteria; ACB07076; ACB07076; Kcr_0318.
DR   GeneID; 6093606; -.
DR   KEGG; kcr:Kcr_0318; -.
DR   eggNOG; arCOG01130; Archaea.
DR   HOGENOM; CLU_017584_4_3_2; -.
DR   InParanoid; B1L3P7; -.
DR   OrthoDB; 9929at2157; -.
DR   PhylomeDB; B1L3P7; -.
DR   Proteomes; UP000001686; Chromosome.
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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACB07076.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001686};
KW   Transferase {ECO:0000313|EMBL:ACB07076.1}.
FT   DOMAIN          37..354
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   359 AA;  40393 MW;  FF3F69CA7EAFE1D5 CRC64;
     MLTIRDVFDA CRRKESEGKR VINAHIGEPS HEPPVQLREL GIGEMGRKYL PFVGTEAARE
     SISHFGSEFL GRDLEKDRIF ITNGGAQSLL ISALAASKIR RGRILVPAPG FPQYFEHASE
     FGYQISTYDP LAEDLVNEVT SKLEGVSGVL INYPNNPTGF VQPNSELMDL WDELRRRNVL
     LINDAAYSQI YFGERVEVVG DIIADTFSKT FALPGLRIGY IYWGAERPEL VGRILYLMTA
     GVSEISQFII MKMIEAASDD YFRRVREHYA KLKDEVIREA RKAGLIFPEP RGAFYLYSMH
     PNVPDSNELA MKLLNRDPVV GIVPAAAFRG GKEYFRISYG VLSEVDIREL FGAIREATS
//