ID A0A0Q4E466_9MICO Unreviewed; 399 AA.
AC A0A0Q4E466;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=ASE56_00065 {ECO:0000313|EMBL:KQM44839.1};
OS Microbacterium sp. Leaf203.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1735677 {ECO:0000313|EMBL:KQM44839.1, ECO:0000313|Proteomes:UP000051381};
RN [1] {ECO:0000313|Proteomes:UP000051381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf203 {ECO:0000313|Proteomes:UP000051381};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf203 {ECO:0000313|Proteomes:UP000051381};
RA Vorholt J.;
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:KQM44839.1}.
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DR EMBL; LMKF01000001; KQM44839.1; -; Genomic_DNA.
DR RefSeq; WP_056223846.1; NZ_LMKF01000001.1.
DR AlphaFoldDB; A0A0Q4E466; -.
DR OrthoDB; 9763453at2; -.
DR Proteomes; UP000051381; 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 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:KQM44839.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051381};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KQM44839.1}.
FT DOMAIN 36..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 399 AA; 42585 MW; 92021CDF53AC6637 CRC64;
MTSRAPLSRK LSAIAESATL KVDAKAKALQ AAGRPVISYA AGEPDFATPS FIVDAAAKAL
QDPKNYRYTP AAGLPVLREA IAAKTLRDSG LEVAPSQVIV TNGGKQSVYQ AFQTVVNPGD
EVLLPAPYWT TYPEAIALAD GTPVEVFAGA DQDYKVTVAQ LEAARTDKTT VLVFVSPSNP
TGSVYTPEET AEIGRWALEH GIWVITDEIY QNLTYEGVKA VSIVEAVPVL AGQTILVNGV
AKTYAMTGWR VGWMVGPADA MKLAGNLQSH LSSNVNNVAQ LAAAAALNGP QDEAEQFRLA
FDRRRQLIVS ELSKIDGVEV PNPLGAFYVY PDVQGLLNRT WGGVTPTTSL ELADLILEQA
EVAVVPGEAF GPSGYLRLSY ALGDDQLLEG IQRLQRLFA
//
