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Database: UniProt
Entry: L8TV50_9MICC
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ID   L8TV50_9MICC            Unreviewed;       453 AA.
AC   L8TV50;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:ELT45621.1};
GN   ORFNames=G205_04021 {ECO:0000313|EMBL:ELT45621.1};
OS   Arthrobacter nitrophenolicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT45621.1, ECO:0000313|Proteomes:UP000011189};
RN   [1] {ECO:0000313|Proteomes:UP000011189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX   PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA   Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT   "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT   Arthrobacter sp. Strain SJCon.";
RL   Genome Announc. 1:e0005813-e0005813(2013).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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:ELT45621.1}.
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DR   EMBL; AOFD01000006; ELT45621.1; -; Genomic_DNA.
DR   AlphaFoldDB; L8TV50; -.
DR   PATRIC; fig|683150.5.peg.813; -.
DR   Proteomes; UP000011189; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ELT45621.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011189};
KW   Transferase {ECO:0000313|EMBL:ELT45621.1}.
SQ   SEQUENCE   453 AA;  49069 MW;  51FBE28A3557DE2D CRC64;
     MSNTIQSIRK PSKAMVNGFD PTRIDELPDE IQKNIRRRDQ SLGPGYRLFY DTPLEVLRGE
     GVKLFDRDGN EYLDVYNNVP SVGHCHPKVI AAVHEQMQTL NTNTRYVQES ILDYSEDLLS
     TFPAELGHVM FTCTGSEAND LAMRVAKYAT GNQGIIVTSG AYHGLTAEVA SFSPSLGIGV
     PLGANVRVID APDALRYSSD QRSLEDHLRN QVRAAIADLH RHGIGLAAFI ADSIFSSDGV
     FAGPAGFLRP IIEEVHAAGG LYIADEVQPG FGRTGQEWWG FQRHGIVPDI VTIGKPMGNG
     IPVAAAIFKP ELLVEFGRNI RYFNTFGGNS VAVAAAQAVL DVIREESLID NALKVGEQII
     TGLEDLAQDL DQVAEVRGSG FFIGVDLVTD RSSLTPDGDA AAGIVNALRE DRILISACGA
     QGNVLKLRPP MPFSSNDADR LLDGIGRAFK RLR
//
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