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Database: UniProt/TrEMBL
Entry: Q2UM29_ASPOR
LinkDB: Q2UM29_ASPOR
Original site: Q2UM29_ASPOR 
ID   Q2UM29_ASPOR            Unreviewed;       498 AA.
AC   Q2UM29;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=AO090003000164 {ECO:0000313|EMBL:BAE57386.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE57386.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE57386.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007155; BAE57386.1; -; Genomic_DNA.
DR   RefSeq; XP_001819388.1; XM_001819336.2.
DR   AlphaFoldDB; Q2UM29; -.
DR   STRING; 510516.Q2UM29; -.
DR   EnsemblFungi; BAE57386; BAE57386; AO090003000164.
DR   GeneID; 5991371; -.
DR   KEGG; aor:AO090003000164; -.
DR   VEuPathDB; FungiDB:AO090003000164; -.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   OMA; FGFECPP; -.
DR   OrthoDB; 5472891at2759; -.
DR   UniPathway; UPA00528; UER00586.
DR   Proteomes; UP000006564; Chromosome 2.
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:UP000006564};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          112..480
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   498 AA;  54920 MW;  95506E4FC2AD22C1 CRC64;
     MATQTTVSYT TTRTLSTPAR CLNPDNINPH VTEAKYAVRG ELAVKAEEYR VKLANGDKSL
     PFDSVIFANI GNPQQLDQKP ITFFRQVLSL LENPQLLNNT EALRTSFFYE QDVVDRAKKL
     LADVQSVGAY SHSQGAPVIR QSIAKFIEER DGFPANPQDL FCCAGASSGV STILNIICNG
     PQAGVLVPIP QYPLYTATLS LLNAQCVPYL LEEQKAWGTD VTAIRNSLAQ ARSTGTDVRS
     IVVINPGNPT GASLSAEDIK NVLDLAAEEK LVVIADEVYQ TNVFEGEFIS FKKRLRQLQQ
     ETPGKYDYVE LVSLHSVSKG MVGECGHRGG YFELVGFDPE VQAQIYKLVS IGLCPPVIGQ
     CLLELMVNPP KEGEGSYELY QKEYNGISEG LHKRAFALYE AFQQMEGVEC QKPQGAMYLF
     PTITLPPKAI EAAKAENRAA DEFYCLRLLD ATGVCVVPGS GFGQKENTLH FRTTFLAPGT
     DWVERIVKFH SEFMAKYK
//
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