ID A0A0Q8VB67_9MICO Unreviewed; 453 AA.
AC A0A0Q8VB67;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KRC50535.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KRC50535.1};
GN ORFNames=ASE16_05820 {ECO:0000313|EMBL:KRC50535.1};
OS Leifsonia sp. Root227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC50535.1, ECO:0000313|Proteomes:UP000051819};
RN [1] {ECO:0000313|EMBL:KRC50535.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC50535.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC50535.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC50535.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Schulze-Lefert P.;
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 -!- 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:KRC50535.1}.
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DR EMBL; LMIO01000002; KRC50535.1; -; Genomic_DNA.
DR RefSeq; WP_055892147.1; NZ_LMIO01000002.1.
DR AlphaFoldDB; A0A0Q8VB67; -.
DR STRING; 1736496.ASE16_05820; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000051819; 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 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:KRC50535.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000051819};
KW Transferase {ECO:0000313|EMBL:KRC50535.1}.
SQ SEQUENCE 453 AA; 47090 MW; 795C2425E4866E9B CRC64;
MTDTLSTSAP VYSVAQERRI VTAVPGPKSQ ELHQRRLAVV PTGVSSTLPV YIAKANGAIL
VDVDGNQFVD FGAGIGVTTV GHTETSVVDA AAAQLQDVIH TLFTITPYEE YVRVAELLAE
HTPGDHAKKT VLVNSGAEAV ENGVKIARKH TGRRAVAVLD HAYHGRTNLT MAMNFKAMPY
ATGFGPFAGD VYHAPSSYPY HDGLTGAEAA ARTIAYLEKV VGASDLACLV VEPIQGEGGF
MVPADGYLPA LQEWCTANGV VFIADEIQSG MARTGAYYAS EHFGLVPDLV LSAKGIAGGL
PLAAVTGRAE IMDSAQPGGL GGTFGGNPVA AAAAVAVFES IEKNDLLDEG KRIEKALKPA
LLALQEKYDI IGDVRGIGAM LAIELVQPGT GATTKEPNAE AVTSIVAYAA QHGVLVLNAG
TYGNVLRFLP SLAVSDALIA DAVQVLDDAF AAL
//
