ID   Q7N2I5_PHOLL            Unreviewed;       404 AA.
AC   Q7N2I5;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=plu3091 {ECO:0000313|EMBL:CAE15465.1};
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE15465.1, ECO:0000313|Proteomes:UP000002514};
RN   [1] {ECO:0000313|Proteomes:UP000002514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01
RC   {ECO:0000313|Proteomes:UP000002514};
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; BX571869; CAE15465.1; -; Genomic_DNA.
DR   RefSeq; WP_011147308.1; NC_005126.1.
DR   AlphaFoldDB; Q7N2I5; -.
DR   STRING; 243265.plu3091; -.
DR   GeneID; 24170090; -.
DR   KEGG; plu:plu3091; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000002514; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000002514}.
FT   DOMAIN          34..391
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45438 MW;  4648DE0ED35F4821 CRC64;
     MLAVKKSSKL DNVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFEA PDEILVDVIR
     NLPTAQGYSD SKGLYSARKA IMQHYQARNM MDVTVEDIYI GNGVSELIVQ AMQALLNTGD
     EMLVPAPDYP LWTAAVSLSS GKAVHYMCDE GSDWFPDLND IRNKITPRTR GIVIINPNNP
     TGAVYSKELL LEVVEIARQH NLIIFADEIY DKILYDDAEH HSIAALAPDL LTVTFNGLSK
     TYRVAGFRQG WMVLNGPKKH AKSYIEGLEM LASMRLCANV PMQHAIQTAL GGYQSISEFI
     LPGGRLYEQR NRAWELINQI PGVSCVKPKG ALYMFPKIDA KRFNVHDDQK MVLDLLLQEK
     VLLVQGTAFN WPEPDHLRIV TLPRLDELEM AIQKFARFIG KYHQ
//