ID A0A0Q6ATL0_9BRAD Unreviewed; 424 AA.
AC A0A0Q6ATL0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KQT28415.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:KQT28415.1};
GN ORFNames=ASG57_17265 {ECO:0000313|EMBL:KQT28415.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT28415.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT28415.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT28415.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT28415.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT28415.1,
RC ECO:0000313|Proteomes:UP000051536};
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:KQT28415.1}.
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DR EMBL; LMQJ01000002; KQT28415.1; -; Genomic_DNA.
DR RefSeq; WP_057195662.1; NZ_LMQJ01000002.1.
DR AlphaFoldDB; A0A0Q6ATL0; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000051536; 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:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:KQT28415.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KQT28415.1}.
SQ SEQUENCE 424 AA; 45128 MW; 8AF6059863C26BA9 CRC64;
MSNASIAARR SEAISRGVGV TTQIYAARAR NSEIWDAEGR RYIDFASGIA VLNTGHCHPK
VIAAAKAQLD QFTHTCHQVV PYENYVRLAE RLNQLVPGSF AKKTIFVTTG AEAVENAVKV
ARAATGRSAV IAFSGGFHGR TFMGMALTGK VAPYKVGFGS MPGDVFHVPF PVALHGISVA
DSLAALERLF KADVDPARVA AVIVEPVQGE GGFYEAPRDF LVALRKICDQ RGILLIADEV
QTGFARTGRM FAMERHGVVA DITTMAKSLG GGFPLAAVTG RAELMDAPGP GGLGGTYGGN
PVGIAAAHAV LDVVEEEKLC DRANLLGARL KQRLESLRED VPEIADIRGP GFMNAIEFND
PVKGVPSEKF AAAVRLKALE KGLILLTCGV YGNVIRFLSP ITIEDSVMHE ALDILEIAIR
HAEA
//
