ID L7ZWF7_9BACI Unreviewed; 585 AA.
AC L7ZWF7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN Name=pgcA1 {ECO:0000313|EMBL:AGE21091.1};
GN ORFNames=GHH_c05500 {ECO:0000313|EMBL:AGE21091.1};
OS Geobacillus sp. GHH01.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1233873 {ECO:0000313|EMBL:AGE21091.1, ECO:0000313|Proteomes:UP000011251};
RN [1] {ECO:0000313|EMBL:AGE21091.1, ECO:0000313|Proteomes:UP000011251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHH01 {ECO:0000313|EMBL:AGE21091.1};
RX PubMed=23618712;
RA Wiegand S., Rabausch U., Chow J., Daniel R., Streit W.R., Liesegang H.;
RT "Complete Genome Sequence of Geobacillus sp. Strain GHH01, a Thermophilic
RT Lipase-Secreting Bacterium.";
RL Genome Announc. 1:E0009213-E0009213(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005164}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004008; AGE21091.1; -; Genomic_DNA.
DR RefSeq; WP_015373995.1; NC_020210.1.
DR AlphaFoldDB; L7ZWF7; -.
DR KEGG; ggh:GHH_c05500; -.
DR PATRIC; fig|1233873.3.peg.542; -.
DR HOGENOM; CLU_016950_0_0_9; -.
DR Proteomes; UP000011251; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd05799; PGM2; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AGE21091.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 43..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..314
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..449
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 492..571
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 585 AA; 65448 MW; 9BE594E5863DA857 CRC64;
MEWRQKYEQW LREPQLDPEL KRLLEQRRHD ERWLEDCFYK NLEFGTGGMR GEIGPGTNRM
NMYTVRKASE GLARYIQSFG DEAKQRGVVI AYDSRHKSPE FAMEAAKTLA TNGIQTYVFD
ELRPTPELSF AVRYLRAFAG IVITASHNPP EYNGYKVYGE DGGQLPPAVA DQVIRYVNEV
ENELAIHVED EKTLREKGLI RIIGSEVDDA YIHAVKTISI HPELARETAI HIVFTPLHGT
SNKPVRRALA ELGYQNVFVV KEQELPDPNF STVASPNPEE HAAFAMAMEL GKQVNADLLI
ATDPDADRLG VAVKNDKGNY VVLTGNQTGG LLLHYLLSQR KAQGTLPENG VVLKTIVTSE
LGRAIAQSFG LETVDTLTGF KFIGEKIKEY EQTGQYVFQF GYEESYGYLI GDFVRDKDAV
QAAVLAAEVC AFYKKQGLSL YEALLQLFDQ YGYYREGQRS LTLKGKEGAE AIAAILASFR
QQPPVEAAGK KVTVIEDYKT KERTNTLTGE KTAINLPTSN VLKYILEDGS WFCLRPSGTE
PKMKAYFGVK GTSLGDSEER LARLTEAVMQ RVKDVLSTVS PSYAQ
//
