ID A0A1Y0RFJ3_9CYAN Unreviewed; 971 AA.
AC A0A1Y0RFJ3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:ARV58743.1};
GN ORFNames=BZZ01_08905 {ECO:0000313|EMBL:ARV58743.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV58743.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV58743.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV58743.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-2017) 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; CP019636; ARV58743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RFJ3; -.
DR KEGG; ncn:BZZ01_08905; -.
DR OrthoDB; 414934at2; -.
DR Proteomes; UP000196302; 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 PRINTS; PR00413; HADHALOGNASE.
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:UP000196302}.
FT DOMAIN 18..251
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 303..686
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 705..733
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 748
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 750
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 748..750
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 764
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 783..788
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 791
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 813
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 851..855
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 882
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 906
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 907
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 907
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 851
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 882
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 971 AA; 109865 MW; 1BACC8FB7274B842 CRC64;
MDKTDYSHHL IYTDWTLTET LLNPNQIHAK ETVFTIGNGY LGTRGSFEEG FPDGLPATFI
HGVYDNVPVV YTELANCPDW LPLVITVDGD RFRMDRGEIL SYERQLDLRR GILSRKVRWR
SPSGKTIDIY FERFASLADQ HVLGLRCQLT PVDFDGLIEV QGSINGYPEN QGFNHWELID
QGKTDQGIWL HLETRTSRIN LGMAAGMTVS GTDAPIQVTN PPGYPTLTTL FQASVGETIT
VDKLVTVFTS RDVDNPVPAA CEKLAQLPSY STLVDAHVQA WDGAWFQSDI TIEGDTKAQL
AVRYNIYQLL ISAPEHDEKV SIPAKTLSGF GYRGHIFWDT EIFILPFFIY TQPKLARNLL
SYRYHTLNGA RRKAVHYGYK EAMYAWESAE TGDEVTPRWL PPNDFYGEDV RIWCRDREIH
ISSDIPYAVW YYWKATGDDE WMRDYGTEII LDTAIFWGSR VEYNTKYERY EIRGVIGADE
YHEFADNNAF TNRLVQWHLE KALLVYEWLR QTYPDRASTL QQKLQITPGR LSRWQDIITN
IWIPSDPSTG LIEQFEGFFQ LEDINLADYE PRDRSMQAIL GIEGANKRQV LKQPDVLMLL
YLMRQSQEFP YTKEILQTNW DYYAPRTDIT YGSSLGPAIH AILASDLGKP KEAYERFMQA
ALVDLENVRG NAADGIHGAS AGGVWQAVIL GFGGVQLAED GPIATPQLPP GWKRLRFKLH
WRGEWHEFDL RPAQDSVIPL DIQGVIFDLD GVLSDTAEYH YLGWQKLADE EGIPFNHQAN
EALRGLSRRE SLLKLVGNRH YSEAQLQEMM DRKNRYYVDF IQTITPKDLL PGTTTLLDEL
KQAGIKIAIG SGSKNARTVI EKLGIAHYID AIADGYSVQR AKPAPDLFLF AGEQLGLEPQ
QCVVFEDATA GVEAALAAGM WAVGLGPAER VGIAHVVLPS LAGVHWSELL DKLRSSVTHV
RGLQPQIKAT T
//
