ID I4NA99_9PSED Unreviewed; 426 AA.
AC I4NA99;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:EIK98389.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:EIK98389.1};
GN ORFNames=PMM47T1_00075 {ECO:0000313|EMBL:EIK98389.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK98389.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK98389.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK98389.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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:EIK98389.1}.
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DR EMBL; AJWX01000001; EIK98389.1; -; Genomic_DNA.
DR RefSeq; WP_008364606.1; NZ_AJWX01000001.1.
DR AlphaFoldDB; I4NA99; -.
DR STRING; 1179778.PMM47T1_00075; -.
DR PATRIC; fig|1179778.3.peg.12; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000004339; 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:EIK98389.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000004339};
KW Transferase {ECO:0000313|EMBL:EIK98389.1}.
SQ SEQUENCE 426 AA; 44845 MW; 229E8ED889526C88 CRC64;
MSKTNESLMQ RRQAAVPRGV GQIHPIFADS AKNATVTDVE GREFIDFAGG IAVLNTGHVH
PKVIAAVEAQ LHKLTHTCFQ VLAYEPYVEV CEKINARVPG DFDKKTLLVT TGSEAVENAI
KIARAATGRA GVIAFTGAYH GRTMMTLGLT GKVVPYSAGM GLMPGGVFRA LYPCELHGIS
VDDSIASIER VFKNDAEPRD IAAIILEPVQ GEGGFYVAPK EFMKRLRALC DQHGILLIAD
EVQTGAGRTG TFFAMEQMGV APDLTTFAKS IAGGFPLAGV CGKAEYMDAI APGGLGGTYA
GSPIACAAAL AVMEVFEEEN LLDRSKAVGE RLVTGLKAIQ AKHPIIGDVR ALGAMIAVEV
FEGADNHKPN AAAVASVVAK ARDKGLILLS CGTYGNVLRI LVPLTAPDEQ LDKGLAIIEA
CFAELA
//
