ID A0A0M2H5H5_9MICO Unreviewed; 453 AA.
AC A0A0M2H5H5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=4-aminobutyrate aminotransferase PuuE {ECO:0000313|EMBL:KJL41586.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KJL41586.1};
GN Name=puuE {ECO:0000313|EMBL:KJL41586.1};
GN ORFNames=RS82_02816 {ECO:0000313|EMBL:KJL41586.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL41586.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL41586.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL41586.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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 -!- 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:KJL41586.1}.
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DR EMBL; JYJA01000037; KJL41586.1; -; Genomic_DNA.
DR RefSeq; WP_045300403.1; NZ_JYJA01000037.1.
DR AlphaFoldDB; A0A0M2H5H5; -.
DR PATRIC; fig|69370.6.peg.2861; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000034098; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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; IPR004632; 4NH2But_aminotransferase_bac.
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 NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:KJL41586.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098};
KW Transferase {ECO:0000313|EMBL:KJL41586.1}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 46556 MW; 692DF1982E712C13 CRC64;
MSSAADTLTE TPLGGPTLPQ ERRLVTSIPG PRSQELLARK ADAVAAGVGH TAPVQAVAAG
GGVIVDADGN SLIDLGSGIA VTTIGNAHPK VVAAVQAQVA QFTHTCFMIA PYDSYVSVAE
ALNRITPGDH AKKSALFNSG AEAVENAVKI ARKYTGKQAV VAFDHGYHGR TNLTMALTAK
SMPYKSGFGP FASEIYRAPL SYPYRDGLDG GLAAKKAISM IEKQVGADNL AAIIIEPIQG
EGGFIVPADG FLPALVEWCR ANDVVFIADE IQTGFARTGE MFASDLFGIV PDLITTAKGI
AGGLPLAAVT GRADIMDASH AGGLGGTYGG NPIACAAALA AIDVFENDGM LERAREIETV
LKGRLQDLRA TDPRVGDVRG HGAMIAAEFV DPATGEPDAA LTAAVAKASI AQGVIVLTCG
TYGNVIRFLP PLSITDDLLH EGMDVVAAAL AAA
//
