ID Q9YFC4_AERPE Unreviewed; 464 AA.
AC Q9YFC4;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 2.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:BAA79272.2};
GN OrderedLocusNames=APE_0317.1 {ECO:0000313|EMBL:BAA79272.2};
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557 {ECO:0000313|EMBL:BAA79272.2, ECO:0000313|Proteomes:UP000002518};
RN [1] {ECO:0000313|EMBL:BAA79272.2, ECO:0000313|Proteomes:UP000002518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1
RC {ECO:0000313|Proteomes:UP000002518};
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA79272.2; -; Genomic_DNA.
DR PIR; D72722; D72722.
DR AlphaFoldDB; Q9YFC4; -.
DR STRING; 272557.APE_0317.1; -.
DR EnsemblBacteria; BAA79272; BAA79272; APE_0317.1.
DR KEGG; ape:APE_0317.1; -.
DR PATRIC; fig|272557.25.peg.246; -.
DR eggNOG; arCOG00767; Archaea.
DR Proteomes; UP000002518; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002518}.
FT DOMAIN 4..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 156..256
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..371
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 388..453
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 464 AA; 49710 MW; AFC383F69CD72B38 CRC64;
MSRRRLFGTD GVRGVIGSEL TPEFVLRLAR AIGAYFGRGS RILVGRDTRS GGELFEGLVA
AGLAFEGVEV HLAGTLPTPA LQLYVRDHGY DAGVMVTASH NPPEYNGIKV VGGDGVEVPR
DVEEGIEALF WEGKFSTVEW RSVAGQPKRV HDAVDYYVNR VVENVSAFTQ RGGGERVVVD
CGGGATSFTT VEILKRLGAR PIPLSCKPDP LFSSRDPEPT PDTLGPAASL VRSSGAVFGV
GHDADGDRAI VIDDRGRVVW GDRSGALLAG FVAEVGLAKG PLKVYTGVSS SIVVEDYLRP
RGIEVVWTPV GAPIIARAIL TQGGIAAFEE NGGYMHPPHQ YVRDGGMKAA LLLAMLRATG
ESLSSLLDRL PSYHPIKTKI PASREEALCA VEAVKQEFQG ERMVTIDGVK VIGEGYWVLV
RPSGTEPVVR IMLEARSEEE ARALFERVLR AVKEKCGIPS GGRT
//
