ID K9TIJ3_9CYAN Unreviewed; 1000 AA.
AC K9TIJ3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:AFY81829.1};
GN ORFNames=Oscil6304_2195 {ECO:0000313|EMBL:AFY81829.1};
OS Oscillatoria acuminata PCC 6304.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=56110 {ECO:0000313|EMBL:AFY81829.1, ECO:0000313|Proteomes:UP000010367};
RN [1] {ECO:0000313|EMBL:AFY81829.1, ECO:0000313|Proteomes:UP000010367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6304 {ECO:0000313|EMBL:AFY81829.1,
RC ECO:0000313|Proteomes:UP000010367};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria acuminata PCC 6304.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR610972-3};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR610972-3};
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DR EMBL; CP003607; AFY81829.1; -; Genomic_DNA.
DR RefSeq; WP_015148472.1; NC_019693.1.
DR AlphaFoldDB; K9TIJ3; -.
DR STRING; 56110.Oscil6304_2195; -.
DR KEGG; oac:Oscil6304_2195; -.
DR PATRIC; fig|56110.3.peg.2597; -.
DR eggNOG; COG0637; Bacteria.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_0_1_3; -.
DR InParanoid; K9TIJ3; -.
DR OrthoDB; 414934at2; -.
DR Proteomes; UP000010367; Chromosome.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01990; bPGM; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR NCBIfam; TIGR02009; PGMB-YQAB-SF; 1.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000010367}.
FT DOMAIN 9..265
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 317..695
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 714..744
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 773
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 775
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 773..775
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 775
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 775
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 789
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 808..813
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 816
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 838
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 876..880
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 907
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 931
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 932
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 932
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 876
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
FT SITE 907
FT /note="Important for catalytic activity and assists the
FT phosphoryl transfer reaction to Asp8 by balancing charge
FT and orienting the reacting groups"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-4"
SQ SEQUENCE 1000 AA; 111876 MW; E0B9587B1626B309 CRC64;
MYATDWTITE RNFDPASEPH HQETVFTLGN GYLGTRGTFE EGYPGAKPAT LINGLYDKVA
IVHTELANCP DWLPMVVSVG GEYFSLDRGE ILHYERQLDM RRGILRRQIR WRSPQGKTLD
LHFERFTSLA EHHIAAIRLS VTPVDFSDIV EIQAGLDGHP DNQGIKHWKW INQGLTPVRT
PQSTNSLPFS LLPSEVDGVW MQLSTLHSGI ELGMATQLSV KNAQQQPLPV LAMTTPGYPT
LTTRFEGNRG ETVTVEKLVT IYTSRETEAP TAEAIAKLSQ LPDYDTLRDE HTAAWDRLWE
KSDVVIEGDL KAQQAIRYNL FQLLQAAPHH DSHVSIPAKT LSGFAYRGHV FWDTEIFLLP
FLSYTQPAIA KNALTYRYHT LPGARRKAAQ SGYEGAMFAW ESAATGDEVT PRWVPDAEGK
ELVRIWCGDI ELHITTDVAY AAWNYWQITG DDAWMVDYGA ELILDTAVFW GSRAEWNGDR
NCYEIRDVIG PDENHDRVNN NTFTNRMMQW HLETAQGVLN WLQDFAPDQA QALVQQLDLN
AKRLTHWNHV IERIYLPTPS QTGLIEQSEG FFALKDVNLA DYEPRQHSMQ AILGIETTNQ
CQILKQPDVL MLLYLLGDRY DSQTLQANWD YYCPRTDHVY GSSLGPAIHA VLAAQLDKPT
EAYEHFMRAA LVDLEDVRGN ACEGIHAAST GGVWQAIVFG FAGIRLTERG PIANPHLPPG
WTRLKFKLSW RDRWYEFDIK QESALADAQK TTSHGSEITA TALRDKLRGV IFDLDGVLTD
TAEYHYLGWK QLADEEGIPF DREANEAMRG LARRESLLTL LGSRQVPEAQ MQEMMDRKNR
YYVDLVAEIG PQDLLPGAME FLMELQAAGI QVAIGSSSKN AHMVVERLGI GHLVQAIADG
YSVSRSKPAP DLFLHAAELL GIPSSQCIVF EDADSGVEAA KAAGMLAIGL GPVERFQDAD
LVLPSLEYIQ WTDLLDKLAQ TALLSGDLAA IGDRIGAGSL
//
