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
//