ID A0A1M6GVK9_9FLAO Unreviewed; 576 AA.
AC A0A1M6GVK9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:SHJ13890.1};
GN ORFNames=SAMN05443429_11040 {ECO:0000313|EMBL:SHJ13890.1};
OS Cruoricaptor ignavus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Cruoricaptor.
OX NCBI_TaxID=1118202 {ECO:0000313|EMBL:SHJ13890.1, ECO:0000313|Proteomes:UP000184335};
RN [1] {ECO:0000313|EMBL:SHJ13890.1, ECO:0000313|Proteomes:UP000184335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25479 {ECO:0000313|EMBL:SHJ13890.1,
RC ECO:0000313|Proteomes:UP000184335};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQYI01000010; SHJ13890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6GVK9; -.
DR STRING; 1118202.SAMN05443429_11040; -.
DR Proteomes; UP000184335; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184335}.
FT DOMAIN 47..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..310
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..444
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 517..559
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT COILED 546..573
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 576 AA; 64396 MW; BC9B216DA2A5F5DB CRC64;
MVNELTSLER AQLWLGESFD EETRTAVEML INSKSPDLDD SFYRALEFGT GGMRGIMGVG
TNRLNKYTLG QATQGLANYL HEQFPNEEIK VAIAYDVRNN SKEFAKIVTD VLTANGIKVL
LFKNHRPTPE LSFTVRNKKC NAGIVLTASH NPPEYNGYKV YWNDGAQVVP PHDENIIKAV
YDTQYEMINF NGNDELIEWI GEEQDEVYID ACIENSLYQK EKTGYENLNI VFTSIHGTTY
ATVPRALEKA GFKKVDLVEE QMVPSGNFPT VESPNPEEPA ALGMAMDLAR ITNADIVIGT
DPDGDRLGIA VRNLNGEMQL LNGNQTNTIL IYYILDQWKK SGKITGREFI GSTIVTSDIF
FDIAEKFGVT CKAGLTGFKW IGKMIRDAEG TEKFVCGGEE SFGFMTGDFV RDKDSCGSIL
LACEIAALCK AQGSSMFEYL IEIYKQVGIY SEGLINVVKK GREGAEEIQL MMKNFRENPP
KELAGSPVEI VEDYKEQTST NIRNNATSVM DEIPKSNVLI WYTEDGTKVC VRPSGTEPKI
KFYVSVKDSL ENIADYETKM ENLKNKIQQV RASLNL
//
