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
//