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Database: UniProt
Entry: I0XVW2_9LEPT
LinkDB: I0XVW2_9LEPT
Original site: I0XVW2_9LEPT 
ID   I0XVW2_9LEPT            Unreviewed;       409 AA.
AC   I0XVW2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Aminotransferase, class I/II {ECO:0000313|EMBL:EIE03020.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:EIE03020.1};
GN   ORFNames=LEP1GSC185_1618 {ECO:0000313|EMBL:EIE03020.1};
OS   Leptospira licerasiae serovar Varillal str. VAR 010.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE03020.1, ECO:0000313|Proteomes:UP000004889};
RN   [1] {ECO:0000313|EMBL:EIE03020.1, ECO:0000313|Proteomes:UP000004889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VAR 010 {ECO:0000313|EMBL:EIE03020.1};
RX   PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA   Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA   Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA   Vinetz J.M., Matthias M.A.;
RT   "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT   Leptospiral Evolution and Pathogenicity.";
RL   PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EIE03020.1}.
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DR   EMBL; AHOO02000005; EIE03020.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0XVW2; -.
DR   PATRIC; fig|1049972.3.peg.940; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000004889; Unassembled WGS sequence.
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; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF19; AROMATIC AMINO ACID AMINOTRANSFERASE DDB_G0272014; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:EIE03020.1};
KW   Transferase {ECO:0000313|EMBL:EIE03020.1}.
FT   DOMAIN          73..399
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   409 AA;  46601 MW;  3008EA7F16B23EF6 CRC64;
     MYKQNKKMGK LILENSSEIF RPSTRTERTP ASVTRDILKV IDTPGMISFA GGLPDDSLFP
     IQDLRNIFET SVSKKGSKLF QYADTQGHFD LRAWIAERYY PGSNADEILL TAGSQQALDL
     LSRYFIEEGS TILLERPSYL GAVQVFSSYA PSFLGINYTE EGPDIEELKY ALRNSAEKPK
     FFYCIPDFQN PSAYSYSLEI RNSISKLLLE NEVPILEDTA YRELYFEEEL PVSLCELGPE
     HTISIGTFSK TLAPALRVGW IKAPKRILKD LIVQKQSMDL HSPTLNQELV YGFVSSSKYE
     EHLSLIRSVY GKKAIHTFSY LKNNFGDSIP LQISKGGLFY WLEFPQEINT DLLFQKCLEK
     GLATVPGSSF FVGKPERNHL RWNFSNASEE ETKLGIERLF EVYKNLPNF
//
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