ID A0A3B0B1Y9_9MICO Unreviewed; 457 AA.
AC A0A3B0B1Y9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aminotransferase class V-fold PLP-dependent enzyme {ECO:0000313|EMBL:RKN66472.1};
GN ORFNames=D7252_01910 {ECO:0000313|EMBL:RKN66472.1};
OS Microbacterium sp. CGR2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1805820 {ECO:0000313|EMBL:RKN66472.1, ECO:0000313|Proteomes:UP000278458};
RN [1] {ECO:0000313|EMBL:RKN66472.1, ECO:0000313|Proteomes:UP000278458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGR2 {ECO:0000313|EMBL:RKN66472.1,
RC ECO:0000313|Proteomes:UP000278458};
RA Mandakovic D., Cintolesi A., Maldonado J., Cortes M.P., Mendoza S.,
RA Aite M., Gaete A., Saitua F., Cambiazo V., Agosin E., Siegel A., Maass A.,
RA Gonzalez M., Latorre M.;
RT "Comparative genome-scale metabolic modeling of two Microbacterium species
RT isolated from Atacama Desert.";
RL Submitted (SEP-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|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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:RKN66472.1}.
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DR EMBL; RBHX01000001; RKN66472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0B1Y9; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000278458; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:RKN66472.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000278458};
KW Transferase {ECO:0000313|EMBL:RKN66472.1}.
FT MOD_RES 293
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 457 AA; 49312 MW; E671B2A2D5FCD95D CRC64;
MSADRMHAAS PESTAIVDAV LDYSRRRMLA TDVPLDKPQT EAELHRLVGA TITNSGLGAH
RALSVFEHIL APACLTTSHP LYLSFIPTAP TMAAIAFDLV VSASGLYGGS WLEGAGAVHA
ENEVLSFLAR EFGLPDTAGG VFVQGGTIGN LSALVAAREA AKARLVGSGK ELPPRWKIVC
SVEAHSSNKS AAKVMDADVV LVQAGEDGVL RADAVREALA EHGDEVCAVV VTAGSTNFGI
VDDIAGIAAL KDEFAFWLHI DGAYGLTAML SPEARPIFAG VERADSVIVD PHKWLFAPFD
CCALIYRDPA DGRRAHTQHA EYLDTLTEAD EFSPSDYSIQ LTRRPRGLPM WFSLATYGVD
AYREAVGGTI ALTKQIAEEI ARRPELRLVR DPQLSVVVFE RDGWERVDYD RWSAALLDSQ
RAFVVPSSHR GCPNTRFAIL NPLTTFDDLV GILDTMK
//
