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Database: UniProt
Entry: Q2JK67_SYNJB
LinkDB: Q2JK67_SYNJB
Original site: Q2JK67_SYNJB 
ID   Q2JK67_SYNJB            Unreviewed;       385 AA.
AC   Q2JK67;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase family protein {ECO:0000313|EMBL:ABD02928.1};
GN   OrderedLocusNames=CYB_1979 {ECO:0000313|EMBL:ABD02928.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02928.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD02928.1, ECO:0000313|Proteomes:UP000001938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; CP000240; ABD02928.1; -; Genomic_DNA.
DR   RefSeq; WP_011433567.1; NC_007776.1.
DR   AlphaFoldDB; Q2JK67; -.
DR   STRING; 321332.CYB_1979; -.
DR   KEGG; cyb:CYB_1979; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_6_0_3; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000001938; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABD02928.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938};
KW   Transferase {ECO:0000313|EMBL:ABD02928.1}.
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         191
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   385 AA;  41679 MW;  3CB83349B91FA13A CRC64;
     MTEEPIPLLD LTGQYRALAG LLQPQLEALL ASGQYIGGAA VQRFEEQFAQ FLGGGPLEAV
     GCNSGTDALV LALQALGIQA GDEVLTSAFS FFASAAAISR VGARPVFVDV DPCTFNLDPQ
     LLERSISCRT KAVVVVHLFG QAANMTQILA IARRHGLAVV EDCAQAVGAC WGGRPVGTWG
     EVGCFSFFPT KNLGAAGDGG AVVTRDPQLA RRVRALREHG QTRPYHHEHL GLNSRLDALQ
     AVILSVKLPY LREWNWRRQG IAECYHRLLQ GIPGLMLPQV GVGGNSVWHQ YTVRVVGSEA
     TDGRRRDYLQ QGLKERGIGS RVYYPLPLPL QPVYRGLGYR RGDLPNAELC AAQVLSLPCF
     PELTTCQQER VAAAIAEILS EKTCP
//
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