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Database: UniProt
Entry: A0A369ULZ9_9GAMM
LinkDB: A0A369ULZ9_9GAMM
Original site: A0A369ULZ9_9GAMM 
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
//
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