ID M1ITS8_9CREN Unreviewed; 454 AA.
AC M1ITS8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:AGE70754.1};
GN ORFNames=SacN8_03910 {ECO:0000313|EMBL:AGE70754.1};
OS Sulfolobus acidocaldarius N8.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1028566 {ECO:0000313|Proteomes:UP000011281};
RN [1] {ECO:0000313|EMBL:AGE70754.1, ECO:0000313|Proteomes:UP000011281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N8 {ECO:0000313|EMBL:AGE70754.1,
RC ECO:0000313|Proteomes:UP000011281};
RX PubMed=22418622; DOI=10.1038/ismej.2012.20;
RA Mao D., Grogan D.;
RT "Genomic evidence of rapid, global-scale gene flow in a Sulfolobus
RT species.";
RL ISME J. 6:1613-1616(2012).
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; CP002817; AGE70754.1; -; Genomic_DNA.
DR RefSeq; WP_011277678.1; NC_020246.1.
DR AlphaFoldDB; M1ITS8; -.
DR GeneID; 78441153; -.
DR KEGG; sacn:SacN8_03910; -.
DR PATRIC; fig|1028566.6.peg.765; -.
DR HOGENOM; CLU_016950_7_1_2; -.
DR Proteomes; UP000011281; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
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};
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 3..133
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..254
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..369
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 391..450
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 454 AA; 50118 MW; 60A1E4AA829E7421 CRC64;
MGKLFGTDGV RGLINKDLSP ELVLKLSRAI GSFFGKGSKL LVGRDVRAGG DMYVKLVEAG
LLSTGVDVFY GGLAPTPTLQ YAVKTLGYDA GVIVTASHNP PEYNGIKVID KDGVEIRREK
ENEIEEILFS ERFNSIEWKA LTNDVKKEDR VIPTYVKGIL QHVDTEKISK KGYTVLIDSA
NSVGGLTSPL VAKELGCKVY TLNGNLDPLF PARMPEPTFE SLKETAKIAL TLKADLSIAH
DGDADRAIFL DSEGRVQWGD RSGTLLSYWS HVKNPKGSRV IVTAVSSSSL TEEYLAKYGL
EVLWTKVGSV DIAHKLQDEK GLAGFEENGG FIYPPHQYVR DGAMSFALML EFMASENLSS
AQLFDRLPKY YLVKTKVNLK PQYDIQGLYG DLIKSYGNRG KVITIDGVKI IGEDFWFLVR
KSGTEPIIRI IVEAKDESKA MLLAEELKKF VESK
//
