ID   G0S8Z8_CHATD            Unreviewed;       488 AA.
AC   G0S8Z8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=CTHT_0044020 {ECO:0000313|EMBL:EGS19909.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS19909.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00025708}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000256|ARBA:ARBA00025785}.
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DR   EMBL; GL988043; EGS19909.1; -; Genomic_DNA.
DR   RefSeq; XP_006694794.1; XM_006694731.1.
DR   AlphaFoldDB; G0S8Z8; -.
DR   STRING; 759272.G0S8Z8; -.
DR   GeneID; 18258440; -.
DR   KEGG; cthr:CTHT_0044020; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OMA; FGFECPP; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 1.10.287.1970; -; 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; IPR045088; ALAT1/2-like.
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; PTHR11751; ALANINE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11751:SF29; ALANINE TRANSAMINASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          110..469
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   488 AA;  53960 MW;  B1A1D8A41F1EA262 CRC64;
     MASEATSSRR LNIDNINPHV RAAKYAVRGE LAVKSEEYRA RLAQGATDLP FDTVISANIG
     NPQQLDQKPI TFFRQVLSIL ENPGLLEKKD VLIEHLGYKT DVIERAEWLL KEVGSVGAYS
     ASNGVPAIRK SVAEFLERRD GFPANWQDIY LSAGASSAVN TLLHIICADK NTGVLVPIPQ
     YPLYTASLSV LDAQCVPYYL NESTNWGTDL NVLKEACEKA KAEGVDVRAV VIINPGNPTG
     ASLPESDIRA VIEFARQERL VIIADEVYQT NVFIGEFISF KKMLRQMQKE QPGVYDNIEL
     ASLHSVSKGM VGECGHRGGY FELVGFDPAV QQEIYKFVSI MLCAPVIGQC LVELMVNPPK
     PGEPSYDLYR AEYDAIFNGL RERANALHAA FEQMEGVECG VPQGSMYLFP RIKLPAKACE
     AAAAEGRTPD EFYCMRMLEA TGVCVVPGSG FGQEPGTLHF RTTFLAPGTE WVGRIVKFHQ
     EFMDKYRD
//