ID A0A1I4B9Y7_9PROT Unreviewed; 544 AA.
AC A0A1I4B9Y7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=SAMN02745775_10552 {ECO:0000313|EMBL:SFK64811.1};
OS Falsiroseomonas stagni DSM 19981.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Falsiroseomonas.
OX NCBI_TaxID=1123062 {ECO:0000313|EMBL:SFK64811.1, ECO:0000313|Proteomes:UP000199473};
RN [1] {ECO:0000313|EMBL:SFK64811.1, ECO:0000313|Proteomes:UP000199473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19981 {ECO:0000313|EMBL:SFK64811.1,
RC ECO:0000313|Proteomes:UP000199473};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; FOSQ01000005; SFK64811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4B9Y7; -.
DR STRING; 1123062.SAMN02745775_10552; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000199473; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199473}.
FT DOMAIN 14..153
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 199..287
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 297..408
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 56823 MW; BA8F0D97FC91A4E6 CRC64;
MPIRQVATTP FADQRPGTSG LRKKVPVFQQ PHYVENFLQS ILDVVGDKLR GATLVIGGDG
RYLNRQVAET AIRMAAAAGA GRILVGQGGL LSTPAASALI RASGAIGGIV LSASHNPGGP
DGDFGIKFNT ANGGPAPEEV TEAIHRRAAA LTAYRIAAEA APDIDAIGET RLLDSIVAVI
DPVAGHAALM ETLVDFPAIA AMFAAGFRMR FDAMSAVTGP YAKAIIEGRL GAPAGTVVNA
TPLPDFGGHH PDPNPVHAAD LMAEMMGDAP PDFGAASDGD GDRNMIVAPG MFVTPSDSLA
ILAAHAHRAP GYAAGLAGVA RSMPTSRAVD RVAKRLGIPS YETPTGWKFF ANLLDSGRIT
LCGEESAGTG SNHVREKDGL WAVLIWLTII AATGRRADAI VRDHWAEFGR DYYSRHDYEE
VDSDAAKALM AALRDKLPTL AGQSFAGLTV AEADDFAYAD PVDGSVTPAQ GVRILFAEDA
RAVFRLSGTG TVGATLRVYL ERFEPDAARH ALPVQEVLAP VIAAAREIAQ IAAHTGRAEP
SIIT
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