ID A0A1I4PTS3_9PSED Unreviewed; 416 AA.
AC A0A1I4PTS3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:SFM31169.1};
GN ORFNames=SAMN04487858_10277 {ECO:0000313|EMBL:SFM31169.1};
OS Pseudomonas sp. ok602.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1761898 {ECO:0000313|EMBL:SFM31169.1, ECO:0000313|Proteomes:UP000199362};
RN [1] {ECO:0000313|Proteomes:UP000199362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK602 {ECO:0000313|Proteomes:UP000199362};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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|RuleBase:RU003560}.
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DR EMBL; FOUL01000002; SFM31169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4PTS3; -.
DR STRING; 1761898.SAMN04487858_10277; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000199362; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; 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 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:SFM31169.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:SFM31169.1}.
SQ SEQUENCE 416 AA; 44171 MW; 16A6A6783453A282 CRC64;
MSSDSISRSI SIVHPIRLSH GKNAEVWDTD GKRYIDFVGG IGVLNLGHCH PSIVQAICAQ
ATRLTHYAFN AAPHAPYIEL MDRLAAFIPL SYPVSGMLTN SGAEAAENAL KMVRGATGRT
AVIAFDGAFH GRTLATLNLN GKVAPYKQKV GTLPGPVYHL PFPSPDNDVT CAEALKALER
LFSVEIDIDD VACFIFEPVQ GEAGFLAMDP AFAQALRRLC DEKGIVLIAD EIQSGFGRTG
QRFAFSRLGI EPDLILLGKS IAGGVPLGAV VGRQALVDAL PKGGLGGTYS GNPIACAAAL
ATLDEMSDAN LQAWGALQEE LILRHYQAWR TDHLCPYLGR LTGVGAMRGI ELINPDGTPA
ARQLTQLLAL AREAGLLLMP SGKSRHIIRL LAPLTTPAAV LEEGLEILGA CLAKLT
//