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}.
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; 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
//