ID Q3KGV6_PSEPF Unreviewed; 403 AA.
AC Q3KGV6;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Putative aminotransferase {ECO:0000313|EMBL:ABA73000.1};
GN OrderedLocusNames=Pfl01_1257 {ECO:0000313|EMBL:ABA73000.1};
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA73000.1, ECO:0000313|Proteomes:UP000002704};
RN [1] {ECO:0000313|EMBL:ABA73000.1, ECO:0000313|Proteomes:UP000002704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA73000.1,
RC ECO:0000313|Proteomes:UP000002704};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP000094; ABA73000.1; -; Genomic_DNA.
DR RefSeq; WP_011332810.1; NC_007492.2.
DR AlphaFoldDB; Q3KGV6; -.
DR KEGG; pfo:Pfl01_1257; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_1_6; -.
DR Proteomes; UP000002704; Chromosome.
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 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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43586:SF24; BLR4730 PROTEIN; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABA73000.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000313|EMBL:ABA73000.1}.
FT DOMAIN 57..383
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 403 AA; 43359 MW; 55B7DB60A27E7A6D CRC64;
MNIDDLSRLR AATPGCAQVV HFNHAGASLP SQATLDAVIE QLQREALGGP MEAADNRVQA
RARNAAAALL NAQPEDIAFA SSGSAAWSQA FNALGPWQPG ERILVGRHEW AGNLACMAEA
VKAGARLEVI PCDAHGAVDP QALAQMIDSQ VRLIALTWLP ANGGLINPAA QIGNVARRHG
IPYFIDAGQA LGQLPCDVQD LQCDVLKGAG RKFLRGPRGT ALMYIRAQFL QRLLPVQRDV
LSAPWDGKRF TLRDDARRFE TSEVSLALLA GLANALEEHN RLGAFAIRQR IAHLSNGLRQ
RLKAIPGLTL RNLGAANQQS GLIAFTLEGW DSVALKQTLA ERRINIGANG VAYTPLDMQA
RGLTNIARVA LSYLNTEEEI DVLLENLTEL AARPQISIST QSP
//
