ID   A0A0J8VA37_9GAMM        Unreviewed;       404 AA.
AC   A0A0J8VA37;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=C9I94_16705 {ECO:0000313|EMBL:PSW23260.1};
OS   Photobacterium swingsii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=680026 {ECO:0000313|EMBL:PSW23260.1, ECO:0000313|Proteomes:UP000240481};
RN   [1] {ECO:0000313|EMBL:PSW23260.1, ECO:0000313|Proteomes:UP000240481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24669 {ECO:0000313|EMBL:PSW23260.1,
RC   ECO:0000313|Proteomes:UP000240481};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (JAN-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSW23260.1}.
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DR   EMBL; PYLZ01000009; PSW23260.1; -; Genomic_DNA.
DR   RefSeq; WP_048899111.1; NZ_PYLZ01000009.1.
DR   AlphaFoldDB; A0A0J8VA37; -.
DR   STRING; 680026.AB733_12725; -.
DR   OrthoDB; 9803354at2; -.
DR   Proteomes; UP000240481; Unassembled WGS sequence.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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   Aminotransferase {ECO:0000313|EMBL:PSW23260.1};
KW   Transferase {ECO:0000313|EMBL:PSW23260.1}.
FT   DOMAIN          35..390
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45442 MW;  4A5BC0C2A2AEE2B6 CRC64;
     MQNIGMSSKL NNVCYDIRGP VLKHAKRMEE EGQKILKLNI GNPAPFGFDA PDEILVDVIR
     NLPTSQGYCD SKGIYPARKA VVQHYQKRGL LDLDVEDVYI GNGVSELIVM AMQALLNNQD
     EILVPSPDYP LWTAAVSLSG GNPVHYICDE QSDWYPDLDD IKKKITPNTR GIVLINPNNP
     TGAVYSRDFL LEVVEIARKH KLIIFADEIY DKILYDGAQH TSIAPLAEDV FCITFNGLSK
     SYRVCGFRAG WMVLSGPKNI AKGYIEGLEM LASMRLCANV PMQHAIQTAL GGYQSINELI
     LPGGRLLEQR NKAYELITQI PGVSCVKPKG ALYLFPKLDQ KKFNIVDDQR MALDFLQQEK
     VLLVHGTGFN WKQPDHFRIV TLPRVDDLEV AIGRLERFLH NYRQ
//