ID D4B3D2_ARTBC Unreviewed; 597 AA.
AC D4B3D2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-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=ARB_02969 {ECO:0000313|EMBL:EFE30178.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE30178.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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}.
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:EFE30178.1}.
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DR EMBL; ABSU01000033; EFE30178.1; -; Genomic_DNA.
DR RefSeq; XP_003010818.1; XM_003010772.1.
DR AlphaFoldDB; D4B3D2; -.
DR STRING; 663331.D4B3D2; -.
DR GeneID; 9524933; -.
DR KEGG; abe:ARB_02969; -.
DR eggNOG; KOG0258; Eukaryota.
DR HOGENOM; CLU_014254_3_0_1; -.
DR OMA; FGFECPP; -.
DR OrthoDB; 5472891at2759; -.
DR UniPathway; UPA00528; UER00586.
DR Proteomes; UP000008866; 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; AT04676P; 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:UP000008866};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 96..463
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 547..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 65668 MW; 87FF77A8102FF7C0 CRC64;
MATPRMNRTN INPNVINAQY AVRGELAVKA EEYRLALERG EKLPFDKVIF ANIGNPQQLE
QKPITFSRQV LSLLEYPPLL QNEEALKSTF GYKSDVIARA KTLLADVQSV GAYSQSLGAP
GIRQSVADFI ARRDGFPASQ KDIYLTGGAS AGVSTILNVI CAGKKTGVLV PIPQYPLYTA
TLSLLDATCV PYYLNESQSW ATDVEEIKTS LANGEKAGTD IRAIVIINPG NPTGASLNPA
AIKDVIDIAA EKSLVIIADE VYQTNVFKGE FTSFKKRLRE LQAEFPGKYD GIELVSLHSV
SKGMVGECGH RGGYFELVGF KPEVVEQVYK FVSINLCPPV IGQCLLECMV HPPVEGEESY
ELYQKEYNSI ADGLKQRAFA LYEAFKKMEG VECQEPQGAM YLFPTIHLPP KAVDAATKAG
RKADEFYCLR LLDATGVCVV PGSGFGQKEG TLHFRTTFLA PGTDWVDRIV KFHGEFMNEF
RDPLCLTSIP VVIVSQSTVA LSSTKYSFLR SNVSTEFTNS RPNSYMQPLS SQPCKLLLRD
KPAIAPANSK FHPDSPRGEP GNRRQLNLGD SEKHPELTVD LSIRKASRIK MLEVLCT
//