ID   A0A0H3YT10_STUST        Unreviewed;       403 AA.
AC   A0A0H3YT10; F8H2W0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=G7024_09105 {ECO:0000313|EMBL:MBA1304565.1};
OS   Stutzerimonas stutzeri (Pseudomonas stutzeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Stutzerimonas.
OX   NCBI_TaxID=316 {ECO:0000313|EMBL:MBA1304565.1, ECO:0000313|Proteomes:UP001138621};
RN   [1] {ECO:0000313|EMBL:MBA1304565.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=109A1 {ECO:0000313|EMBL:MBA1304565.1};
RA   Mcfarland A.G., Bertucci H.K., Litmann E., Shen J., Huttenhower C.,
RA   Hartmann E.M.;
RT   "Synteny-based analysis reveals conserved mechanism for high triclosan
RT   tolerance in Pseudomonas, as well as instances of horizontal transfer.";
RL   Submitted (FEB-2020) 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:MBA1304565.1}.
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DR   EMBL; JAAMRD010000005; MBA1304565.1; -; Genomic_DNA.
DR   RefSeq; WP_011913649.1; NZ_WWNS01000006.1.
DR   GeneID; 66820826; -.
DR   OMA; CALDLCI; -.
DR   Proteomes; UP001138621; Unassembled WGS sequence.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004069; F:L-aspartate: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:MBA1304565.1};
KW   Transferase {ECO:0000313|EMBL:MBA1304565.1}.
FT   DOMAIN          34..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   403 AA;  44804 MW;  7C89AA8EF533EB2E CRC64;
     MQVSKSNKLA NVCYDIRGPV LKHAKRLEEE GHRILKLNIG NPAPFGFEAP EEILQDVIRN
     LPTAQGYSDS KGLFSARKAI MQYYQQKQVE GIGIEDIYLG NGVSELIVMS MQALLNNGDE
     VLIPAPDYPL WTAAVSLAGG KPVHYLCDEQ ANWWPDLADI KAKITPNTKA LVLINPNNPT
     GAVYPKEVLE GMVELARQHK LVLFSDEIYD KILYDGAVHI STASLAPDVL CLTFNGLSKS
     YRVAGFRSGW VAISGPKHKA QSYIEGLDIL ANMRLCANVP SQHAIQTALG GYQSINDLVL
     PPGRLLEQRN RTWELLNDIP GISCVKPMGA LYAFPRIDPK ICPIHNDEKF VLDLLLSEKL
     LIVQGTAFNW PWPDHFRVVT LPRVDDLEQA IGRIGNFLKT YQQ
//