ID A0A2T1C0Z0_9CYAN Unreviewed; 969 AA.
AC A0A2T1C0Z0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:PSB01793.1};
GN Name=pgmB {ECO:0000313|EMBL:PSB01793.1};
GN ORFNames=C7B64_16520 {ECO:0000313|EMBL:PSB01793.1};
OS Merismopedia glauca CCAP 1448/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC Merismopedia.
OX NCBI_TaxID=1296344 {ECO:0000313|EMBL:PSB01793.1, ECO:0000313|Proteomes:UP000238762};
RN [1] {ECO:0000313|EMBL:PSB01793.1, ECO:0000313|Proteomes:UP000238762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1448/3 {ECO:0000313|EMBL:PSB01793.1,
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:PSB01793.1, ECO:0000313|Proteomes:UP000238762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1448/3 {ECO:0000313|EMBL:PSB01793.1,
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 -!- 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};
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:PSB01793.1}.
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DR EMBL; PVWJ01000088; PSB01793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1C0Z0; -.
DR OrthoDB; 414934at2; -.
DR Proteomes; UP000238762; Unassembled WGS sequence.
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; 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 Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000238762}.
FT DOMAIN 14..253
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 305..690
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 709..739
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 753
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 755
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 753..755
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 769
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 788..793
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 796
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 818
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 856..860
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 887
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 911
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 912
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 912
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 856
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 887
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 969 AA; 110405 MW; 910271EDFEE434CB CRC64;
MEALGWTVVE SKLDYKQAQE ALFTIGNGYL GTRGALEEGY PSQHPVTLIH GVYDDVPVVY
TELVNCPNWL SWKIKIDGET FRCDSEALLQ ADRGDILHYE RRLDLRSGVL LREVTWRSPR
GHTVELRFER FASISDRHVL AQRCQIKSVD FAATVEFEAQ IDSEVDNQGL NHWEDLKQGD
SNLNDQELGI WLEARTSKSE IQLAMAAKLV VADAEAEILA QHNPGCPSLT TQFFIHPGQT
VNLEKLVTVF TSREVDDPKQ SAWDKLQDLP SYMTLLAPQM ATWRQIWENS DVLIEGDLKA
QLAVRYNLFQ LLIAAPRHDD TVSIPAKTLS GFGYRGHVFW DTEIFILPFF IYTQPELARN
LLMYRYRTLP GARRKAQEGG YEGALFAWES AGTGDEVTPR WVPDKTGEMI RIWCRDIELH
INTDVAYGVW KYWQVTGDDA WLQDYGAEII LDTAIFWASR VEWNRDRLCY EISDVIGPDE
NHEHVDNNAF TNGMVRWHLE RALQLWSWLE QRDSAFAAQL ARKINLTDTR LSKWVEIVQK
IEVKQDQETC LIEQFDGFLN LEDVNLTDYE PRSESMQAIL GISETNQRQI LKQPDVLMLL
YLLGDHYEDD GSACSRERTL ATNWDYYHQR TDRSYGSSLA PAIHSILASQ MQQPQAAYED
FMQAALVDLD NLRGNTAEGI HGACAGGVWQ AIVFGFAGVR LTPNGFTTQP QLPPGWTRLK
FRLQWQEQWY EFDLRPQNTQ PSTMPEIQGV IFDLDGVLTD TADFHYLGWK QLADEMNIPF
DSQINEGMRG LPRRESLLHI LGDRQVPAVE FEEMMERKNG YYLKLIEGIS PDNLLPGVRS
LLEQLRSHQI KIGIGSSSKN ARMVLEKLGI AEFIEAIADG YSVSRPKPAP DLFLHAANLL
HLEPEKCLVV EDAGAGVEAA LAANMWALGV GPHERLGHAH LVLPSLENTS WEDLQRRLNE
VRSQFRFAI
//
