ID   A0A8J8CHV1_9CYAN        Unreviewed;       388 AA.
AC   A0A8J8CHV1;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   29-MAY-2024, entry version 10.
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}.
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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|ARBA:ARBA00022679, 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
//