ID Q2JSH2_SYNJA Unreviewed; 386 AA.
AC Q2JSH2;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=DegT/DnrJ/EryC1/StrS aminotransferase family protein {ECO:0000313|EMBL:ABD00403.1};
GN OrderedLocusNames=CYA_2266 {ECO:0000313|EMBL:ABD00403.1};
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321327 {ECO:0000313|EMBL:ABD00403.1, ECO:0000313|Proteomes:UP000008818};
RN [1] {ECO:0000313|EMBL:ABD00403.1, ECO:0000313|Proteomes:UP000008818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABD00403.1,
RC ECO:0000313|Proteomes:UP000008818};
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; CP000239; ABD00403.1; -; Genomic_DNA.
DR RefSeq; WP_011431076.1; NC_007775.1.
DR AlphaFoldDB; Q2JSH2; -.
DR STRING; 321327.CYA_2266; -.
DR KEGG; cya:CYA_2266; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_3; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000008818; 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:ABD00403.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:ABD00403.1}.
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 386 AA; 42230 MW; FD5CB0A0AB66FC49 CRC64;
MTDEPIPLLD LTLQYRALAE TLLPEVEALL ASGQYIGGEA VRRFEELFSR FLGGGDLEAV
GCNSGTDALV LALRALGIQA GDEVITTAFS FFASAEAIDL VGARPVFVDV DPCTFNLDPQ
LLEKSISPRT KAVIPVHLFG QAANMTEILA IARRHGLAVI EDCAQAVGAC WGGRPVGTWG
DIGCFSFFPT KNLGAAGDGG AVVTRDPQLA RKVRILKEHG QTRQYQHEHI GLNSRLDALQ
AVILSVKLTH LREWNWRRQG IAESYHRLLQ GIPGLILPQV AVGGNSVWHQ YTVRVPGSDS
TDSRRRDRLQ KQLQERGIAS RVYYPIPLHL QPVYRKKLGY KPGDLPNAEL CAAQVLSLPC
FPELTLQQQE RVAAAIAQIL TEQTCS
//
