Y1304_SYNY3
ID Y1304_SYNY3 Reviewed; 287 AA.
AC P73599;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable ketose 3-epimerase {ECO:0000305};
DE EC=5.1.3.- {ECO:0000305};
GN OrderedLocusNames=sll1304;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Probably catalyzes the epimerization of ketopentoses and/or
CC ketohexoses at the C3 position. {ECO:0000250|UniProtKB:C1KKR1,
CC ECO:0000250|UniProtKB:Q9WYP7, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9WYP7};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9WYP7};
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17643.1; -; Genomic_DNA.
DR PIR; S77309; S77309.
DR AlphaFoldDB; P73599; -.
DR SMR; P73599; -.
DR IntAct; P73599; 1.
DR STRING; 1148.1652723; -.
DR PaxDb; P73599; -.
DR EnsemblBacteria; BAA17643; BAA17643; BAA17643.
DR KEGG; syn:sll1304; -.
DR eggNOG; COG1082; Bacteria.
DR InParanoid; P73599; -.
DR OMA; GLAMESF; -.
DR PhylomeDB; P73599; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..287
FT /note="Probable ketose 3-epimerase"
FT /id="PRO_0000209113"
FT ACT_SITE 152
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 246
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
SQ SEQUENCE 287 AA; 32848 MW; DACA991588B97E40 CRC64;
MISSPKIKFG VHTFIWKKEF LGNEEYVFQD AKRWGFDGIE IATHYFDQID PLQLKSYGEK
YGVELTFCTS LPRGLSLTTK DEDCWRESIA YLERAIKFCQ QCGIIQLSGP FPHPVGYLSG
EPLQKRENVR MQEAFKLVAE TLIKTDLKFA VEPLNRFQGY ALNTVAQGLE LLDAVDCPQL
GLLLDLFHMN IEEKDVIKAF LQASNHCFHI HACAKDRGTP GSDSFAWGHW FKALQTMDYQ
GWVTIESFNF EDKELANGAR LWRTVAPSNE ALAQDGLKFL RQTYQTN
