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Database: UniProt
Entry: A0A3T0Y7Z4_9MICC
LinkDB: A0A3T0Y7Z4_9MICC
Original site: A0A3T0Y7Z4_9MICC 
ID   A0A3T0Y7Z4_9MICC        Unreviewed;       411 AA.
AC   A0A3T0Y7Z4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=MN0502_25590 {ECO:0000313|EMBL:BBE23676.1};
OS   Arthrobacter sp. MN05-02.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1571833 {ECO:0000313|EMBL:BBE23676.1, ECO:0000313|Proteomes:UP000283134};
RN   [1] {ECO:0000313|EMBL:BBE23676.1, ECO:0000313|Proteomes:UP000283134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN05-02 {ECO:0000313|EMBL:BBE23676.1,
RC   ECO:0000313|Proteomes:UP000283134};
RA   Ii KM., Kono N., Paulino-Lima IG., Tomita M., Rothschild LJ., Arakawa K.;
RT   "Complete genome sequence of Arthrobacter sp. Strain MN05-02, a UV-
RT   resistant bacteria from Sonoran Desert.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC       ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; AP018697; BBE23676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3T0Y7Z4; -.
DR   Proteomes; UP000283134; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; 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   PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:BBE23676.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283134};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:BBE23676.1}.
FT   DOMAIN          44..399
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   411 AA;  43314 MW;  79B1E68C323F3CC3 CRC64;
     MNATTDDSTR AALPRISRRI DSIAESATLA VDAKAKALKA AGRPVIGFGA GEPDFPTPDY
     IVEAAIAAAR QPKFHRYSPA GGLPDLRQAI AEKTLRDSGY AVDPAQVLVT NGGKQAVYES
     FASLLDPGDE VLVPTPFWTT YPEAIRLAGG VPVEVFAGPE QGYLVTVDQL EAALTPRTKV
     LLFVSPSNPT GAVYGADVVR EIGEWAAARG LWVVTDEIYE HLTYDGVPFT SIATAAPALG
     DRVVILNGVA KTYAMTGWRV GWMVGPKDLV KAATNLQSHA TSNVSNVPQM AALAAVSGPL
     TAVDAMKVAF DRRRRAMVSA LNEIDGVECP TPHGAFYAYA DVRALLGRSF DGVTPATSAE
     LAALILEKVE VAVVPGEAFG PSGYLRLSYA LGDEDLATGV GRLQEFLGSA R
//
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