ID Q2JKM4_SYNJB Unreviewed; 387 AA.
AC Q2JKM4;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Soluble hydrogenase, tritium exchange subunit, putative {ECO:0000313|EMBL:ABD02765.1};
GN OrderedLocusNames=CYB_1808 {ECO:0000313|EMBL:ABD02765.1};
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:ABD02765.1, ECO:0000313|Proteomes:UP000001938};
RN [1] {ECO:0000313|EMBL:ABD02765.1, 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP000240; ABD02765.1; -; Genomic_DNA.
DR RefSeq; WP_011433406.1; NC_007776.1.
DR AlphaFoldDB; Q2JKM4; -.
DR STRING; 321332.CYB_1808; -.
DR KEGG; cyb:CYB_1808; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_1_0_3; -.
DR OrthoDB; 389074at2; -.
DR Proteomes; UP000001938; Chromosome.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000001938}.
FT DOMAIN 28..331
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 194
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 387 AA; 41683 MW; ED8C9327887DBE6A CRC64;
MKDKLILMIP GPTPVPESAL LAMARGPIEH RSKEFTAILE EVTDGLRWLH QTTSDVFVFS
ASGTGAMEAG ILNTLSPGDR VLVGVNGKFG ERWAEMSEQF GLQCERVETP WGIPYPVEIF
QEKLAADREK TIKAVILTHS ETSSGVANDV QAIAAAAREH GEALVLVDGV TSVGAMPVLM
DEWGLDVVAS GSQKGYMIPP GLGFVAVSPR AMAATERSRF PKYYWSFKLA QKALRQGTTP
FTPAVNLFYA LRTTLQMMRA EGLEAIYRRH ARLSQATRAG VKALGLKLLV DPESAASPSV
TAVLAPEGIN ADTLRSTLKK HFDIALAAGQ DHLKGKIFRI GHLGFVSDRD VLMTLAALES
ALHTVGYSDF TPGAGTRAAE EVLAHGF
//
