ID B6SMP5_MAIZE Unreviewed; 458 AA. AC B6SMP5; DT 16-DEC-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 1. DT 27-MAR-2024, entry version 52. DE RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106}; DE EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106}; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG26128.1}; RN [1] {ECO:0000313|EMBL:ACG26128.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4; RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V., RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.; RT "Insights into corn genes derived from large-scale cDNA sequencing."; RL Plant Mol. Biol. 69:179-194(2009). 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 -!- PATHWAY: Photosynthesis; C4 acid pathway. CC {ECO:0000256|ARBA:ARBA00025709}. 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU954010; ACG26128.1; -; mRNA. DR RefSeq; NP_001147214.1; NM_001153742.1. DR AlphaFoldDB; B6SMP5; -. DR UniPathway; UPA00322; -. DR UniPathway; UPA00528; UER00586. DR ExpressionAtlas; B6SMP5; baseline and differential. 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 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; 2. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2. 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:SF440; ALANINE TRANSAMINASE; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 2: Evidence at transcript level; KW Aminotransferase {ECO:0000313|EMBL:ACG26128.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACG26128.1}. FT DOMAIN 150..435 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 458 AA; 50771 MW; 2103947F6AB4D659 CRC64; MSYNKAPSIT AETINPRVKI IRYAPCGEIV KHAARLEQEI EENPASIPFQ EIIYCNLGNP QVLGQPPLTF FREVLSLCDN PALMDRDEAR ALFSPCSIRR ARRILNSIPS KDTGGYTDCR GIKCLRQVVA DGITARDGFP STADDIFLTD GATSAVPYNL TEDNGWGLEI FEVKRCLEEA RSAGLTVRAM VVINPGNPTG QVLSVTNQEE IVEFCRKEGL VILADEVYQE NIYAENKKFH SFKKVARSLA YDENDLTLVS LHFVSMSYGE SGRRGGYMEV SGVAANVKDQ IYKVASLTLC PNIAGQILVS LAMDPPKLGD ESFESFDKEK EQIRSSFCKR AKTLEKAFSG LEGVTCNKLE GALYLFPRLH LPSAAIRAAD FEGVSPDIFY AHRLLDATGI AVVPGSGFHQ ASGTIHIRCT ILPDERKIEV MVARLRAFHK AFMNEFRGSQ QVMNDLRR //