ID A0A2T1C7A6_9CYAN Unreviewed; 330 AA.
AC A0A2T1C7A6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=KpsF/GutQ family sugar-phosphate isomerase {ECO:0000313|EMBL:PSB04139.1};
GN ORFNames=C7B64_05205 {ECO:0000313|EMBL:PSB04139.1};
OS Merismopedia glauca CCAP 1448/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC Merismopedia.
OX NCBI_TaxID=1296344 {ECO:0000313|EMBL:PSB04139.1, ECO:0000313|Proteomes:UP000238762};
RN [1] {ECO:0000313|EMBL:PSB04139.1, ECO:0000313|Proteomes:UP000238762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1448/3 {ECO:0000313|EMBL:PSB04139.1,
RC ECO:0000313|Proteomes:UP000238762};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB04139.1, ECO:0000313|Proteomes:UP000238762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1448/3 {ECO:0000313|EMBL:PSB04139.1,
RC ECO:0000313|Proteomes:UP000238762};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000256|ARBA:ARBA00008165, ECO:0000256|PIRNR:PIRNR004692}.
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:PSB04139.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PVWJ01000017; PSB04139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1C7A6; -.
DR OrthoDB; 9762536at2; -.
DR Proteomes; UP000238762; Unassembled WGS sequence.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd04604; CBS_pair_SIS_assoc; 1.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR NCBIfam; TIGR00393; kpsF; 1.
DR PANTHER; PTHR42745; -; 1.
DR PANTHER; PTHR42745:SF1; ARABINOSE 5-PHOSPHATE ISOMERASE KDSD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW Isomerase {ECO:0000313|EMBL:PSB04139.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR004692-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000238762};
KW Zinc {ECO:0000256|PIRSR:PIRSR004692-2}.
FT DOMAIN 39..182
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 208..268
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 277..330
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-2"
FT SITE 57
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 109
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 150
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
FT SITE 191
FT /note="Catalytically relevant"
FT /evidence="ECO:0000256|PIRSR:PIRSR004692-3"
SQ SEQUENCE 330 AA; 35059 MW; D5C14B27F46B8F7B CRC64;
MTVTGSNIHA SQVLELLKLE AEAITQAAHQ LNPQEVDKAI ALLMHCPGKV ILTGVGKSGI
VARKIAATLT STRTLATYLH PCDALHGDFG IVTGDDVAII LSNSGETEEA VAMLPYLKHR
QVPIIAILGN LNSTLARNAN AVLDASVAKE ACPLNLAPTA STTVAMAIGD ALAMTLVQAK
GLTPEDFALN HPAGRLGKRL TLKVADLMHS GAYNPTISPD SSWLEVVEKI SQAGLGAVNA
IDRDRRLLGI ITDGDLRRAI QQTDPTELGK LYAGKIMTRN PSVVLPTDLA YDALQMMENR
PSQISVLPVV DEDRICVGLI RLHDVVRSGL
//
