ID   A8H481_SHEPA            Unreviewed;       404 AA.
AC   A8H481;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Spea_2048 {ECO:0000313|EMBL:ABV87368.1};
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579 {ECO:0000313|EMBL:ABV87368.1, ECO:0000313|Proteomes:UP000002608};
RN   [1] {ECO:0000313|EMBL:ABV87368.1, ECO:0000313|Proteomes:UP000002608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1 {ECO:0000313|Proteomes:UP000002608};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000851; ABV87368.1; -; Genomic_DNA.
DR   RefSeq; WP_012155284.1; NC_009901.1.
DR   AlphaFoldDB; A8H481; -.
DR   STRING; 398579.Spea_2048; -.
DR   KEGG; spl:Spea_2048; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000002608; 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   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:ABV87368.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002608};
KW   Transferase {ECO:0000313|EMBL:ABV87368.1}.
FT   DOMAIN          35..393
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45132 MW;  0268E6FD7A005639 CRC64;
     MRPIIKSNKL DSVCYDIRGP VHKEARRLED EGHRILKLNI GNPAPFGFEA PEEIVRDVIL
     NLPSAQGYCE SKGLFSARKA IVQHYQSQGI FGVDIEDIYI GNGVSELIVM AMQGLLNSGD
     EVLVPSPDYP LWTAAVHLSG GKAQHYRCDE ESDWFPDLED IKSKITPRTR GLVLINPNNP
     TGAVYSKELI LEVIELCRQN DMILFADEIY DKILYDEAVH IPAASLSDDI LTVTFNGLSK
     VYRAAGFRVG WMMLTGNKKA AKSYVEGLDM LASMRLCANV PSQHAIQTAL GGYQSIQELV
     QPGGRLRVQR DACVEMLNSI PGVSVKTPKG ALYAFAKLDQ KKFNLRDDER LVLDLLKDRK
     ILLVQGSAFN YPEPDHVRVV FLPYKEELTK ALSEFGDFLA NYKQ
//