ID A0A0M2H2F5_9MICO Unreviewed; 451 AA.
AC A0A0M2H2F5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=4-aminobutyrate aminotransferase GabT {ECO:0000313|EMBL:KJL37634.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KJL37634.1};
GN Name=gabT {ECO:0000313|EMBL:KJL37634.1};
GN ORFNames=RS81_03391 {ECO:0000313|EMBL:KJL37634.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL37634.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL37634.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL37634.1,
RC ECO:0000313|Proteomes:UP000033956};
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:KJL37634.1}.
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DR EMBL; JYIZ01000057; KJL37634.1; -; Genomic_DNA.
DR RefSeq; WP_045277259.1; NZ_JYIZ01000057.1.
DR AlphaFoldDB; A0A0M2H2F5; -.
DR STRING; 92835.RS81_03391; -.
DR PATRIC; fig|92835.4.peg.3429; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000033956; 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:KJL37634.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956};
KW Transferase {ECO:0000313|EMBL:KJL37634.1}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 46064 MW; 6E1A237DFD98BD1C CRC64;
MTAADTLTTT PLGGPSLPQE RRLVTSIPGP RSQQLLERKA AAVAAGVGHT APIEAVAAGG
GVVVDADGNS LIDLGSGIAV TSVGNAHPKV VEAVQAQVAQ FTHTCFMVSP YESYVAVAEA
LNRITPGDHA KKSALFNSGA EAVENAIKIA RKFTKKPAVV AFDHGYHGRT NLTMALTAKA
MPYKSGFGPF ASEIYRAPLS YPYRDGLSGA DAAAKAISII EKQVGADNLA AVIIEPIQGE
GGFIVPADGF LPAIVDWCRA NDVVFIADEI QTGFARTGAM FASEIFGIVP DLITTAKGIA
GGLPLAAVTG RAEIMDASHA GGLGGTYGGN PVACAAALAS IEAFETEGLI ERAREIGAIL
TERLTQIQAG DPRVGDVRGH GAMIAAEFVT ADGSPDAALT AAVAKACIAE GVIVLTCGTY
GNVIRFLPPL AITDDLLHEG IDVVAAALAA S
//
