ID   Q48FR1_PSE14            Unreviewed;       403 AA.
AC   Q48FR1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=PSPPH_3631 {ECO:0000313|EMBL:AAZ33743.1};
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ33743.1, ECO:0000313|Proteomes:UP000000551};
RN   [1] {ECO:0000313|EMBL:AAZ33743.1, ECO:0000313|Proteomes:UP000000551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA   Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA   Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA   Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(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; CP000058; AAZ33743.1; -; Genomic_DNA.
DR   RefSeq; WP_011169208.1; NC_005773.3.
DR   AlphaFoldDB; Q48FR1; -.
DR   KEGG; psp:PSPPH_3631; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000000551; 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:AAZ33743.1};
KW   Transferase {ECO:0000313|EMBL:AAZ33743.1}.
FT   DOMAIN          34..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   403 AA;  44923 MW;  3CDD18983AB8BE3A CRC64;
     MQFNKSNKLA NVCYDIRGPV LKHAKRLEEE GHRILKLNIG NPAPFGFEAP DEILQDVIRN
     LPTAQGYSDS KGLFSARKAV MQYYQQKQVE GVGIEDIYLG NGVSELIVMS MQALLNNGDE
     VLVPAPDYPL WTAAVALSGG SPVHYLCDEQ ANWWPDLEDI KAKITPNTKA MVIINPNNPT
     GAVYSREVLL GMLELARQHN LVVFSDEIYD KILYDDAMHI CTASLAPDLL CLTFNGLSKS
     YRVAGFRSGW IAISGPKHNA QSYIEGIDIL ANMRLCANVP SQHAIQTALG GYQSINDLIL
     PPGRLLEQRN RTWELLNDIP GVSCVKPMGA LYAFPRIDPK VCPIFNDEKF VLDLLLSEKL
     LVVQGTAFNW PYPDHFRVVT LPRVDELEQA IGRIGNFLKG YRQ
//