ID A0A166CPZ8_9EURY Unreviewed; 455 AA.
AC A0A166CPZ8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KZX14746.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:KZX14746.1};
GN Name=glmM_1 {ECO:0000313|EMBL:KZX14746.1};
GN ORFNames=MBFIL_08090 {ECO:0000313|EMBL:KZX14746.1};
OS Methanobrevibacter filiformis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=55758 {ECO:0000313|EMBL:KZX14746.1, ECO:0000313|Proteomes:UP000077066};
RN [1] {ECO:0000313|EMBL:KZX14746.1, ECO:0000313|Proteomes:UP000077066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11501 {ECO:0000313|EMBL:KZX14746.1,
RC ECO:0000313|Proteomes:UP000077066};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter filiformis DSM 11501.";
RL Submitted (APR-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}.
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:KZX14746.1}.
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DR EMBL; LWMT01000128; KZX14746.1; -; Genomic_DNA.
DR RefSeq; WP_066971764.1; NZ_LWMT01000128.1.
DR AlphaFoldDB; A0A166CPZ8; -.
DR STRING; 55758.MBFIL_08090; -.
DR PATRIC; fig|55758.3.peg.909; -.
DR OrthoDB; 10363at2157; -.
DR Proteomes; UP000077066; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 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 InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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:KZX14746.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077066}.
FT DOMAIN 6..132
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 258..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 373..432
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 455 AA; 49770 MW; BC9DD9CC33E70921 CRC64;
MTSKKRLFGT FGVRRVANEV LTPEFAARLA ACYGSLVKGK IAIGGDTRTT TSMIKYAISS
GLLSSGCDVV DLGILPTPAV QYAVRNYYDG GIIVTASHNP PKYNGIKFVD EFGIGINDEL
DLAIEELYFD GEPERASWKE IGNLYHNNKI IDEYLEEVIK RVDSDAIKQA KLKVILDPGS
GAGCFTAPYL FRKLGCEIIT LNSQADGFFP GRDPEPIEAN IKDLIDTVIE LKADIGIAHD
GDADRTICID ENGAFVLGDK TFALVEKQML KENNGGLVVT TVATSSAIEE IAIENNGEFI
ATAVGDLIVS RKLKDEDGLF GGEENGGLIF PDFVYGRDAA LSAAKILEII AKEKKPLSEL
VAELPVYYSQ KLKIKCPDEK KDEVMKKIAE EVSSLGFKVD TTDGVKIFKE DGWVIIRPSG
TEPIFRSFSE SKVEKNAIEM AKWGISLIDK YQSTF
//
