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Database: UniProt
Entry: A3YUB0_9SYNE
LinkDB: A3YUB0_9SYNE
Original site: A3YUB0_9SYNE 
ID   A3YUB0_9SYNE            Unreviewed;       373 AA.
AC   A3YUB0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=WH5701_05120 {ECO:0000313|EMBL:EAQ76625.1};
OS   Synechococcus sp. WH 5701.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=69042 {ECO:0000313|EMBL:EAQ76625.1, ECO:0000313|Proteomes:UP000002935};
RN   [1] {ECO:0000313|EMBL:EAQ76625.1, ECO:0000313|Proteomes:UP000002935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH5701 {ECO:0000313|Proteomes:UP000002935};
RA   Scanlan D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {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:EAQ76625.1}.
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DR   EMBL; AANO01000001; EAQ76625.1; -; Genomic_DNA.
DR   RefSeq; WP_006173244.1; NZ_CH724160.1.
DR   AlphaFoldDB; A3YUB0; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_2_3; -.
DR   OrthoDB; 9813612at2; -.
DR   Proteomes; UP000002935; 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; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000002935};
KW   Transferase {ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          47..367
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   373 AA;  40809 MW;  9DF14B6392589114 CRC64;
     MDGGPPEPAA LERHGGNLEA VARRLGCRPA DLLDASASLV PFGPSASVRR VLQAVLRTPA
     GKPSPLRDYP DREQLRLRRA IAAHHQIDPA AVLPGNGAAE LFTWLARDAA AAGTSLLPTP
     GFADYPRALA CWGGVWSPWP LALPRPGPVV WPQPLPSAPA GSLQALWVTN PHNPTGQLWS
     RASLEPLLER FALVIVDEAF LPLVPGGESQ SLLPLVASHP GLVVIRSLTK LLAIAGLRLG
     YAVADPARLR RWAAWRDPWP VNGLAAAVGE ALVGDRLWQE RVQCWVASEG PWLQQRLQQL
     PGLTPLPSAA NFLLLRSESP LVALRERLER HQRVLLRDCR SFDGLGECWL RIALQDRRNN
     RRLLRALRQE ISR
//
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