ID   I3ZLF3_TERRK            Unreviewed;       414 AA.
AC   I3ZLF3;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Terro_3862 {ECO:0000313|EMBL:AFL90071.1};
OS   Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL90071.1, ECO:0000313|Proteomes:UP000006056};
RN   [1] {ECO:0000313|EMBL:AFL90071.1, ECO:0000313|Proteomes:UP000006056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC   {ECO:0000313|Proteomes:UP000006056};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete genome of Terriglobus roseus DSM 18391.";
RL   Submitted (JUN-2012) 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; CP003379; AFL90071.1; -; Genomic_DNA.
DR   RefSeq; WP_014787331.1; NC_018014.1.
DR   AlphaFoldDB; I3ZLF3; -.
DR   STRING; 926566.Terro_3862; -.
DR   KEGG; trs:Terro_3862; -.
DR   PATRIC; fig|926566.3.peg.3803; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_0; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000006056; 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:AFL90071.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW   Transferase {ECO:0000313|EMBL:AFL90071.1}.
FT   DOMAIN          34..395
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   414 AA;  45708 MW;  4AC1E33478CC1D80 CRC64;
     MKKINKSRKL DHVLYDIRGP IMDRAKQMEE EGQQLIKLNI GNLAVFGFEA PEEVRLDMIR
     NLPNSAGYSD SKGIFAARKA VMHYTQTQGI QGVTLDDIYL GNGASELIAM AATALLDDGD
     ELLVPAPDYP LWTAVTSLSG GKPVHYICDE ANGWNPDLDD IRAKITPRTK GIVVINPNNP
     TGVVYPDHIL VGIVAIAREH GLVILADEVY DKVLYDDARH TAMGSLSTDV LTLTFNSLSK
     SYRACGYRSG WMVVSGDKAA GANFIEGLNM LANMKLCANV PGQWAIQTAL GGYQSINDLV
     REGGRLRKQR DLAYELLTAI PGITCVRPQA ALYMFPRLDP AIYPIADDRQ FLLQLLEATR
     VLLVQGTGFN WPNPDHFRIV FLPHETDLRE AIGRIARFLA DYRAKQNPEA ISIS
//