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Database: UniProt
Entry: U1QL27_9EURY
LinkDB: U1QL27_9EURY
Original site: U1QL27_9EURY 
ID   U1QL27_9EURY            Unreviewed;       468 AA.
AC   U1QL27;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ERH07678.1};
GN   ORFNames=J07HN4v3_00040 {ECO:0000313|EMBL:ERH07678.1};
OS   Halonotius sp. J07HN4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halonotius.
OX   NCBI_TaxID=1070774 {ECO:0000313|EMBL:ERH07678.1, ECO:0000313|Proteomes:UP000030639};
RN   [1] {ECO:0000313|EMBL:ERH07678.1, ECO:0000313|Proteomes:UP000030639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J07HN4 {ECO:0000313|Proteomes:UP000030639};
RX   PubMed=23637883;
RA   Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA   Allen E.E.;
RT   "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL   PLoS ONE 8:E61692-E61692(2013).
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; KE356577; ERH07678.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1QL27; -.
DR   eggNOG; arCOG00767; Archaea.
DR   HOGENOM; CLU_016950_7_1_2; -.
DR   Proteomes; UP000030639; 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   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; 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:UP000030639}.
FT   DOMAIN          3..129
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          170..259
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          264..367
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          413..453
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   468 AA;  48642 MW;  D869F558C6246AD7 CRC64;
     MVTFGTAGVR GSATETVTPA VALSVGGAVG HLAVGESTTD HPEIAIGRDG RLTGPALAAA
     VEAGVAATGA IPIRVGTVPT PTLAFASRDR YGVMLTASHN PPADNGIKCF VDGQEFDDDR
     EKRIESLVAD DVATTPTDFA EWGSPQHREP LAAYRTAVVD YVREQLATDG EADLCDGLRV
     AVDCGNGMAA LATPQVLDSL GATVVALNAN VDGRFPGRPS KPTPETLSDF RAFMTDSAFD
     LGIAHDGDAD RIVILDGDGG IVHEDTIVAM LAGYYTRQSS TEQGVGDPVV VTTPNASGRI
     DEVVADAGGR VERVRLGALH EGIAAAENGG DVVFAAEPWK HIHPAFGGWI DGVVSAALLT
     GLVAADGLAD LRRPITERPY RKVSVDCPES AKQPAMTTLE SSLSEAFPDA TVSLEHGVRL
     TLPDSSWLLV RPSGTEPYIR LYAESGSVDD IVATATKQIE AAIDVATG
//
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