ID   B5FFL3_ALIFM            Unreviewed;       404 AA.
AC   B5FFL3;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=VFMJ11_1798 {ECO:0000313|EMBL:ACH66186.1};
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH66186.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACH66186.1, ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|EMBL:ACH66186.1,
RC   ECO:0000313|Proteomes:UP000001857};
RX   PubMed=19182778; DOI=10.1038/nature07660;
RA   Mandel M.J., Wollenberg M.S., Stabb E.V., Visick K.L., Ruby E.G.;
RT   "A single regulatory gene is sufficient to alter bacterial host range.";
RL   Nature 458:215-218(2009).
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; CP001139; ACH66186.1; -; Genomic_DNA.
DR   RefSeq; WP_005419982.1; NC_011184.1.
DR   AlphaFoldDB; B5FFL3; -.
DR   GeneID; 77252939; -.
DR   KEGG; vfm:VFMJ11_1798; -.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000001857; Chromosome I.
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   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:ACH66186.1};
KW   Transferase {ECO:0000313|EMBL:ACH66186.1}.
FT   DOMAIN          35..389
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45005 MW;  75BBAE7D85353DDF CRC64;
     MQNIGMSSKL SSVCYDIRGP VLKHAKRMEE EGHKILKLNI GNPAPFGFDA PDEILVDVIK
     NLPTSQGYCD SKGIYSARKA VVQHYQRRGL LDLDVEDVYI GNGASELIVM AMQALLNNGD
     EMLVPAPDYP LWTAAVSLSG GKPVHYMCDE GADWYPDLDD IKKKITPNTK GIVLINPNNP
     TGAVYSRDFL LQVVEIARQN NLIIFADEIY DKVLYDGAVH TTLATLAPDI LTVTFNGLSK
     AYRVCGFRGG WMFLNGPKDH AQGYIAGLDM LASMRLCANV PMQHAIQTAL GGYQSINELL
     LPGGRLLEQR DKAYDLITQI PGVSCVKPKG AMYLFPKLDP KMYKIKDDQK FVLDFLIKEK
     VLLVQGTGFN WPTPDHFRIV TLPRVDDLET AIGRLERFLH TYKQ
//