ID Q4K8U4_PSEF5 Unreviewed; 403 AA.
AC Q4K8U4;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN OrderedLocusNames=PFL_4247 {ECO:0000313|EMBL:AAY93503.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY93503.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY93503.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CP000076; AAY93503.1; -; Genomic_DNA.
DR RefSeq; WP_011062521.1; NC_004129.6.
DR AlphaFoldDB; Q4K8U4; -.
DR STRING; 220664.PFL_4247; -.
DR GeneID; 57477315; -.
DR KEGG; pfl:PFL_4247; -.
DR PATRIC; fig|220664.5.peg.4346; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_2_6; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AAY93503.1};
KW Transferase {ECO:0000313|EMBL:AAY93503.1}.
FT DOMAIN 34..394
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 403 AA; 44795 MW; 68DD4E0E12E699FC CRC64;
MQVSKSNKLA NVCYDIRGPV LKHAKRLEEE GHRILKLNIG NPAPFGFEAP DEILQDVIRN
LPTAQGYSDS KGLFSARKAV MQYYQQKQVE GIGIEDIYLG NGVSELIVMA MQALLNNGDE
VLVPAPDYPL WTAAVSLAGG NPVHYLCDEQ ANWWPDLADI KAKITPNTKA LVIINPNNPT
GAVYPREVLL GMLELARQHN LVVFSDEIYD KILYDDAVHI CTASLAPDLL CLTFNGLSKS
YRVAGFRSGW VAISGPKQHA QSYIEGIDML ANMRLCANVP SQHAIQTALG GYQSINDLVL
PPGRLLEQRN RTWELLNDIP GVSCVKPMGA LYAFPRIDPK ICPIHNDEKF VLDLLLSEKL
LVVQGTAFNW PWPDHFRVVT LPRVDDLEQA IGRIGSFLKS YRQ
//
