ID   Q7MMF8_VIBVY            Unreviewed;       404 AA.
AC   Q7MMF8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=VV1114 {ECO:0000313|EMBL:BAC93878.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC93878.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC93878.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC93878.1,
RC   ECO:0000313|Proteomes:UP000002675};
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA   Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA   Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000037; BAC93878.1; -; Genomic_DNA.
DR   RefSeq; WP_011080966.1; NC_005139.1.
DR   AlphaFoldDB; Q7MMF8; -.
DR   STRING; 672.VV93_v1c10350; -.
DR   KEGG; vvy:VV1114; -.
DR   PATRIC; fig|196600.6.peg.1110; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_6; -.
DR   Proteomes; UP000002675; 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:BAC93878.1};
KW   Transferase {ECO:0000313|EMBL:BAC93878.1}.
FT   DOMAIN          35..393
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45339 MW;  53DAF78D70706E95 CRC64;
     MQNIGMSSKL DNVCYDIRGP VLKHAKRMEE EGHKILKLNI GNPAPFGFDA PDEILVDVIR
     NLPTSQGYCD SKGIYSARKA VVQHYQRKGI RSLDVEDVYV GNGVSELIVM AMQALLNNGD
     EMLVPAPDYP LWTAAVALSG GKAVHYLCDE QADWYPDLDD MRKKITPKTR GIVLINPNNP
     TGAVYSRDFL LEVIEIARQH KLMIFADEIY DKVLYDGAVH TSVATLTDDV LVMTFNGLSK
     AYRVCGFRGG WMFMTGPKHL AQGYVNGLDM LASMRLCANV PMQHAIQTAL GGYQSINELI
     LPGGRLLEQR DRAWELINQI PGVSCVKPKG AMYLFPKIDT KKYSIKDDQK MVFDFLVQEK
     VLLVQGSGFN WPKPDHFRIV TLPHIEDLET AIGRFERFLH GYSQ
//