ID A0A8J8CHV1_9CYAN Unreviewed; 388 AA. AC A0A8J8CHV1; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 27-MAR-2024, entry version 9. DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481}; DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481}; GN ORFNames=GS601_00765 {ECO:0000313|EMBL:NDJ15831.1}; OS Myxacorys almedinensis A. OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae; OC Myxacorys; Myxacorys almedinensis. OX NCBI_TaxID=2690445 {ECO:0000313|EMBL:NDJ15831.1, ECO:0000313|Proteomes:UP000646053}; RN [1] {ECO:0000313|EMBL:NDJ15831.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A {ECO:0000313|EMBL:NDJ15831.1}; RA Tiago I., Soares F., Portugal A.; RT "High-Quality draft genome sequences of three cyanobacteria isolated from RT the limestone walls of the Old Cathedral of Coimbra."; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|RuleBase:RU000481}; CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441, CC ECO:0000256|RuleBase:RU000481}. 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:NDJ15831.1}. 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; WVIE01000001; NDJ15831.1; -; Genomic_DNA. DR Proteomes; UP000646053; Unassembled WGS sequence. 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 CDD; cd00609; AAT_like; 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; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000481, KW ECO:0000313|EMBL:NDJ15831.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000646053}; KW Transferase {ECO:0000256|RuleBase:RU000481}. FT DOMAIN 31..380 FT /note="Aminotransferase class I/classII" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 388 AA; 41921 MW; B24F65A51B8FE6E2 CRC64; MKLAARVSQV TPSLTLAIDA KAKAMKRDGV DVCSFSAGEP DFDTPDHIKQ AASEALKQGK TRYGPAAGEP KLRDAIALKL QTDNQLCYSA ENIIVTNGGK HSLYGLMMAL IEPGDEVIIP VPFWVSYPEM VKLAGGTPVM VNTTAAAHYK ITPDQLRAAI TPKTKLFVLN SPSNPTGMVY TPGEIRAIAQ VIVENDILVV SDEIYEKLLY DGADHLSIGA ASPEVFDRTI ISHGFAKAYS MTGWRVGYLA APVEIIKAAT KIQGHSTSNV CTFAQYGAIA AYQGSQDCVE QMRQAFAERR QVIVDLVKAM PGLTCIKPDG AFYLLINISK VGMTSLDFCD QLLTDHQVAA IPGIAFGTDD HIRLSYATDL TTIERGMERL SAFVTSKV //