ID S7U3C0_9BACI Unreviewed; 379 AA.
AC S7U3C0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:EPR28564.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:EPR28564.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:EPR28564.1};
GN ORFNames=I656_01760 {ECO:0000313|EMBL:EPR28564.1};
OS Geobacillus sp. WSUCF1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=886559 {ECO:0000313|EMBL:EPR28564.1, ECO:0000313|Proteomes:UP000014961};
RN [1] {ECO:0000313|EMBL:EPR28564.1, ECO:0000313|Proteomes:UP000014961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSUCF1 {ECO:0000313|EMBL:EPR28564.1,
RC ECO:0000313|Proteomes:UP000014961};
RX PubMed=23950119;
RA Bhalla A., Kainth A.S., Sani R.K.;
RT "Draft Genome Sequence of Lignocellulose-Degrading Thermophilic Bacterium
RT Geobacillus sp. Strain WSUCF1.";
RL Genome Announc. 1:e00595-13(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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:EPR28564.1}.
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DR EMBL; ATCO01000074; EPR28564.1; -; Genomic_DNA.
DR AlphaFoldDB; S7U3C0; -.
DR PATRIC; fig|886559.3.peg.1672; -.
DR Proteomes; UP000014961; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EPR28564.1};
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 2..53
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 75..173
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 177..288
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 294..369
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 379 AA; 42638 MW; C702FD1B8CA114CE CRC64;
MFYYSLYYTN IPCGMIITAS HNPGDENGFK IAMGKTTIYG ERIQALRRAM ERLSQEQPRP
ETARGREETL DLAPAYINML KEKIKLGPRK LKVVVDCGNG TPSIIAPQVL KEWGCDVVPL
YCESDPTFPN HHPDPVVPEN LTDLIEMVRK EQADLGIAFD GDGDRIGVVD ETGAIRWGDQ
LMVLFWREIL KRHPGADAPV EVKCSQALVE EIERLGGKPF FHRTGHSHVK ATLRRRPEIP
FAGEMSGHLF FNDEFYGYDD ALYAAGRLLR LLSHDERPLS EWFADVPRYA ATPETRVACP
EEKKAAAIAA VKNRFAGRYP VIDVDGARIQ FPEGWGLVRP SNTQPILVLR AEAKTEVALA
EIKRQLADCL ATLELRIDW
//
