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Database: UniProt
Entry: A0A0Q9QZI9_9MICC
LinkDB: A0A0Q9QZI9_9MICC
Original site: A0A0Q9QZI9_9MICC 
ID   A0A0Q9QZI9_9MICC        Unreviewed;       411 AA.
AC   A0A0Q9QZI9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=ASH00_01325 {ECO:0000313|EMBL:KRF08397.1};
OS   Arthrobacter sp. Soil782.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF08397.1, ECO:0000313|Proteomes:UP000053496};
RN   [1] {ECO:0000313|EMBL:KRF08397.1, ECO:0000313|Proteomes:UP000053496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil782 {ECO:0000313|EMBL:KRF08397.1,
RC   ECO:0000313|Proteomes:UP000053496};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF08397.1, ECO:0000313|Proteomes:UP000053496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil782 {ECO:0000313|EMBL:KRF08397.1,
RC   ECO:0000313|Proteomes:UP000053496};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRF08397.1}.
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DR   EMBL; LMSO01000001; KRF08397.1; -; Genomic_DNA.
DR   RefSeq; WP_056543966.1; NZ_LMSO01000001.1.
DR   AlphaFoldDB; A0A0Q9QZI9; -.
DR   STRING; 1736410.ASH00_01325; -.
DR   OrthoDB; 4436468at2; -.
DR   Proteomes; UP000053496; Unassembled WGS sequence.
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:KRF08397.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KRF08397.1}.
FT   DOMAIN          43..398
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   411 AA;  43661 MW;  925D159CFE05DF2B CRC64;
     MTAADALSQH SNGRVSQRIG AIAESATLAV DARAKALKAA GRPVIGFGAG EPDFPTPDYI
     VDAAVDAARQ PRFHRYSPAG GLPELKQAVA EKTLRDSGYE VDPAQVLVTN GGKQAVYESF
     ATLLDPGDEV LVPTPYWTTY PEAIRLAGGV PVEVFAGPEQ SYLVSIDQLE AARTPRTKIL
     LFVSPSNPTG SVYSPEQVRE IGEWAAGHGL WVVTDEIYEH LTYDDVPFTS IATAAPSLGD
     RVVILNGVAK TYAMTGWRVG WMIGPKDVVK AATNLQSHAT SNVANVSQMA ALAAVSGPLT
     AVEEMKKSFD RRRRAMVSGL NEIDGIQCPT PHGAFYAYAD VRELLGRELA GARPATSAEL
     AALILDTVEV AVVPGEAFGP SGYLRLSYAL GDEDLATGVG RLQEFLGTAR H
//
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