ID   G0GB44_SPITZ            Unreviewed;       415 AA.
AC   G0GB44;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=Spith_0792 {ECO:0000313|EMBL:AEJ61068.1};
OS   Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ61068.1, ECO:0000313|Proteomes:UP000007254};
RN   [1] {ECO:0000313|EMBL:AEJ61068.1, ECO:0000313|Proteomes:UP000007254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700085 / DSM 6578 / Z-1203
RC   {ECO:0000313|Proteomes:UP000007254};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Spirochaeta thermophila DSM 6578.";
RL   Submitted (JUN-2011) 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; CP002903; AEJ61068.1; -; Genomic_DNA.
DR   RefSeq; WP_014624445.1; NC_017583.1.
DR   AlphaFoldDB; G0GB44; -.
DR   STRING; 869211.Spith_0792; -.
DR   KEGG; stq:Spith_0792; -.
DR   HOGENOM; CLU_017584_4_2_12; -.
DR   OrthoDB; 367386at2; -.
DR   Proteomes; UP000007254; 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:AEJ61068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007254};
KW   Transferase {ECO:0000313|EMBL:AEJ61068.1}.
FT   DOMAIN          36..400
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   415 AA;  46749 MW;  858729384B4A268E CRC64;
     MKQLFQKSHK LDDVCYEIRG PVMDEARRME EEGFQILKLN IGNPAPFGFN TPDEILHDII
     INLPNAQGYG DSKGIFPARK AVMQYYQAKG VFDADTDYIF IGNGVSELIS ISLQALLNPE
     DEVLIPAPDY PLWTAVTRLA GGRPVHYICD EESDWIPDID DIRRKITSRT KGIVVINPNN
     PTGAVYPREV LEKIYEIACE HNLVIFSDEI YEKIIYDEDA RAAYSPMSLI AEDALCLTFN
     GLSKAYRAAG LRAGWLMISG KKRPFAKDYI EGISLLSNMR LCSNMTAQFG IQTALGGYQS
     IDDLVRPGGR LYEQRNLCYE LLNQIPGVSC RKPKGALYCF PKLDAERFGI ESDELFVLDF
     LREKKVQVVQ GTGFNWPHPD HFRIVFLPDK DTLRDAIGRL ADFLADYRQN GAGVA
//