ID K9VVT5_9CYAN Unreviewed; 967 AA.
AC K9VVT5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:AFZ12223.1};
DE EC=2.4.1.230 {ECO:0000313|EMBL:AFZ12223.1};
DE EC=5.4.2.6 {ECO:0000313|EMBL:AFZ12223.1};
GN ORFNames=Cri9333_1325 {ECO:0000313|EMBL:AFZ12223.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ12223.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ12223.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ12223.1,
RC ECO:0000313|Proteomes:UP000010472};
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 Crinalium epipsammum PCC 9333.";
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; CP003620; AFZ12223.1; -; Genomic_DNA.
DR RefSeq; WP_015202345.1; NC_019753.1.
DR AlphaFoldDB; K9VVT5; -.
DR STRING; 1173022.Cri9333_1325; -.
DR KEGG; cep:Cri9333_1325; -.
DR PATRIC; fig|1173022.3.peg.1438; -.
DR eggNOG; COG0637; Bacteria.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_0_1_3; -.
DR OrthoDB; 414934at2; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033831; F:kojibiose phosphorylase activity; IEA:UniProtKB-EC.
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; IPR041492; HAD_2.
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; PF13419; HAD_2; 1.
DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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 Glycosyltransferase {ECO:0000313|EMBL:AFZ12223.1};
KW Isomerase {ECO:0000313|EMBL:AFZ12223.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Transferase {ECO:0000313|EMBL:AFZ12223.1}.
FT DOMAIN 10..242
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 294..671
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 690..718
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="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
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 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 967 AA; 108709 MW; 5FA1F42763087C88 CRC64;
MESFGWTVIE SQFDPTHLHH QETVFTLGNG YLGTRGSFEE GYPGECSTTL IHGVYDDIPV
VYTELVNCPN WLPIVITIGG ETFRLDQGQT LHYQRQLDLR LGLLSREIRW RSPAGHTVDI
YFERFTSLAD QHVLVQRCQV TSVDFTGEIE IQASINGEVD NQGVKHWEFV EQSITDNTLW
LHTRTLNSAI DLAIAAKLLI VDFPAEIQAL RTQNCPGLGT TVQIQPGQTI TLEKLVTVFT
SRDRVDPVGE ALGLLNCLPS YTTVFAAHVA AWAKVWQDSD IVIEGDLKAQ LAVRYNIFQL
LAVAPRHDNR VSIPAKTLSG YAYRGHIFWD TEIFIVPFLT LTQPALARNL LTYRYKTLAG
ARRKAQEAGY EGALFAWESA KTGDEVTPRW VPGPDGKIIR IWCSDIELHI NNDIAYAVWH
YWQNTGDDAW MREYGAEIIL DTANYWASRA EWNKERGAYE ISDVIGPDEY HEKINNNAFT
NGMVQWHLQT ALGVWDWLTR SDSDRATILK QQLKLNKKRF QQWAEISQNL VFNQNADTGL
IEQFDGFFDL KDVPLTEYEP RTKSMQVILG IEGANQQQVL KQPDVLMLLY LLRDRTNRQT
LQTNWDYYNP RTDHTYGSSL GPAIHAILGC ELGQPEEAYK HFMRSALVDL EDVRGNANEG
IHAASAGGVW QALIFGFAGV KLTPEGPISS PHLPPGWTRL KFRLQWRNQW YEFDIQESAT
SDQQSAMISS STSNSQLATP NIKGVIFDLD GVITDTADFH YLGWKRITDE EGIPYDWETN
EKMRGLTRRD SLLYILGDKK VSEATIQDMM ERKNNYYLEL IKEMTPDKLL PGVLNLLNEL
RAAGIKVALG SSSKNAHLVL QRLGIEDKFD AIADGYSVEN PKPAPDLFLH AAAQLNLSPE
ECVVIEDATA GVEAALSAGM YAVGLGPVER VGDADVVLPN LEGVQWSDLL TQIAVSSQSS
DVRSLKV
//
