ID A0A369ULZ9_9GAMM Unreviewed; 1029 AA.
AC A0A369ULZ9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Beta-phosphoglucomutase {ECO:0000313|EMBL:RDD80620.1};
DE EC=5.4.2.6 {ECO:0000313|EMBL:RDD80620.1};
GN Name=pgmB {ECO:0000313|EMBL:RDD80620.1};
GN ORFNames=DVJ77_16710 {ECO:0000313|EMBL:RDD80620.1};
OS Dyella tabacisoli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=2282381 {ECO:0000313|EMBL:RDD80620.1, ECO:0000313|Proteomes:UP000253782};
RN [1] {ECO:0000313|EMBL:RDD80620.1, ECO:0000313|Proteomes:UP000253782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L4-6 {ECO:0000313|EMBL:RDD80620.1,
RC ECO:0000313|Proteomes:UP000253782};
RA Zhou X.-K., Li W.-J., Duan Y.-Q.;
RT "Dyella tabacisoli L4-6T, whole genome shotgun sequence.";
RL Submitted (JUL-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:RDD80620.1}.
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DR EMBL; QQAH01000016; RDD80620.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369ULZ9; -.
DR OrthoDB; 9816160at2; -.
DR Proteomes; UP000253782; Unassembled WGS sequence.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProt.
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:SF13; GLYCOSYL TRANSFERASE-RELATED; 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; 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 Isomerase {ECO:0000313|EMBL:RDD80620.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR610972-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR610972-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000253782}.
FT DOMAIN 28..281
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 341..716
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 726..784
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT ACT_SITE 819
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-1"
FT BINDING 817..819
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 819
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 819
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 833
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 852..857
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 860
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 884
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 922..926
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 953
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-2"
FT BINDING 977
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 978
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT BINDING 978
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR610972-3"
FT SITE 922
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 953
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 1029 AA; 112590 MW; 01AA23F1F5061BEC CRC64;
MLDHHESESV NASAPHDGKP IDPWLLTRHG IDPAGFAQDE SLFALANGAL GVRGGLEEGD
SPTQASFLAA AWERTPIEYH ERFPGFASHT DTRIPVADAT RIQLRLGNTP VRLGEGHWLD
FERALDLRNG RYCRRLRWRS PTGATLEIEA ERIVSLADPG LLAIRYQVRS IDYHGPISFE
SSISTTRAAA EQGLDPRIGA RLDGGLNTGN ARADEAQAWL QQQTTHSGIR LACAQAHAWP
GSELSFRQAH LSAHGVTQTY AGTLAPGQTI ALEKYVAYAW TQPDGTDSDG ALLARAEASL
LRAAQHGYAT LLDRQTEILA KLWQDTDLAI DGDPQIEQAL RFNLFHVFQS SGRDGHSSAA
AKGLTGEGYE GHYFWDAEAF MLPALVNLAP ELAHGMLLYR YRTLDRSRRH ARELNHPRGA
LYAWRTISGD ECSAYFPGGS AQYHINAAVA WAVRLYVDAS GDHEFMLKHG AEMLFETARI
WLDIGHFNPR RGGAFCIHEV TGPDEYSALV DNNHYTNRMA QRHLRDAAAT ALWMLNSAPA
AYAALCARIE LGEGEITKWR RAAEAMYLPV DTRLGIFPQD DGFLDKPRLR HADGDVDVDV
DVDHQDAHAK RPLLLKLHPL SIYRHQVCKQ ADTLLALMLA GETVDRDAKR RNFDYYEGVT
VHDSTLSAST FSVIAAEIGE AAKAYRYFLD TLRVDLDDLH GNAAHGVHMA AMAGSWLALT
WGFGGLRVID GLPSLAPRLP DAWRGYRFGL RWRDVQLRVA VDRDGVTYTL SRGIELNFRH
HGQAKHLRSG ESLRLAHSMP APSRHRLTQP LQAVIFDLDG VIADTAVAHD AAWRQLAAEI
GVPFDDSLGE RLKGVDRMGS LALLLERSQH AYSDAEKTAL AERKNTYYKA RIADMGPQDL
LPGARAAIES ARRAGLKIGL ASASRNAPML LQRLGITELF DYVVDASRIV HSKPDPEIFL
AAASGLGIAP SACLGVEDAA AGIASLRAAG MTAVGVGLHE ALADADVLLP SVAAFDISIF
KTDSNGELG
//