PGMB_BACSU
ID PGMB_BACSU Reviewed; 226 AA.
AC O06995;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Beta-phosphoglucomutase;
DE Short=Beta-PGM;
DE EC=5.4.2.6;
GN Name=yvdM; OrderedLocusNames=BSU34550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-224, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "The crystal structure of beta-phosphoglucomutase from bacillus subtilis.";
RL Submitted (JUL-2010) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the interconversion of D-glucose 1-phosphate (G1P)
CC and D-glucose 6-phosphate (G6P), and forming beta-D-glucose 1,6-
CC (bis)phosphate (beta-G16P) as an intermediate. The beta-
CC phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. It
CC plays a key role in the regulation of the flow of carbohydrate
CC intermediates in glycolysis and the formation of the sugar nucleotide
CC UDP-glucose (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucose 1-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:20113, ChEBI:CHEBI:57684, ChEBI:CHEBI:58247;
CC EC=5.4.2.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: The catalysis proceeds via a phosphoenzyme formed by
CC reaction of an active-site nucleophile with the cofactor glucose 1,6-
CC diphosphate (G1,6-diP). The phosphorylated mutase binds either G1P or
CC G6P and transfers the phosphoryl group to the C(6)OH or C(1)OH,
CC respectively (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; Z94043; CAB08042.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15460.1; -; Genomic_DNA.
DR PIR; E70034; E70034.
DR RefSeq; NP_391335.1; NC_000964.3.
DR RefSeq; WP_003228210.1; NZ_JNCM01000033.1.
DR PDB; 3NAS; X-ray; 3.00 A; A/B=2-224.
DR PDBsum; 3NAS; -.
DR AlphaFoldDB; O06995; -.
DR SMR; O06995; -.
DR STRING; 224308.BSU34550; -.
DR PaxDb; O06995; -.
DR PRIDE; O06995; -.
DR DNASU; 938624; -.
DR EnsemblBacteria; CAB15460; CAB15460; BSU_34550.
DR GeneID; 938624; -.
DR KEGG; bsu:BSU34550; -.
DR PATRIC; fig|224308.179.peg.3742; -.
DR eggNOG; COG0637; Bacteria.
DR InParanoid; O06995; -.
DR OMA; ANGYHIV; -.
DR PhylomeDB; O06995; -.
DR BioCyc; BSUB:BSU34550-MON; -.
DR EvolutionaryTrace; O06995; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR CDD; cd02598; HAD_BPGM; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR InterPro; IPR010972; Beta-phosphoglucomutase.
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 Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01990; bPGM; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..226
FT /note="Beta-phosphoglucomutase"
FT /id="PRO_0000108051"
FT ACT_SITE 9
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 7..9
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 42..47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114..118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 114
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:0000250"
FT SITE 145
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:0000250"
FT MOD_RES 7
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3NAS"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3NAS"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:3NAS"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 66..85
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3NAS"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3NAS"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3NAS"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3NAS"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:3NAS"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3NAS"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3NAS"
FT HELIX 209..221
FT /evidence="ECO:0007829|PDB:3NAS"
SQ SEQUENCE 226 AA; 25102 MW; 593851AE23BF9DA7 CRC64;
MKAVIFDLDG VITDTAEYHF LAWKHIAEQI DIPFDRDMNE RLKGISREES LESILIFGGA
ETKYTNAEKQ ELMHRKNRDY QMLISKLTPE DLLPGIGRLL CQLKNENIKI GLASSSRNAP
KILRRLAIID DFHAIVDPTT LAKGKPDPDI FLTAAAMLDV SPADCAAIED AEAGISAIKS
AGMFAVGVGQ GQPMLGADLV VRQTSDLTLE LLHEEWEQYR IRESIP
