ID   A0A202EBT1_9EURY        Unreviewed;       470 AA.
AC   A0A202EBT1;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:OVE85743.1};
GN   ORFNames=B2G88_02700 {ECO:0000313|EMBL:OVE85743.1};
OS   Natronolimnobius baerhuensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronolimnobius.
OX   NCBI_TaxID=253108 {ECO:0000313|EMBL:OVE85743.1, ECO:0000313|Proteomes:UP000196084};
RN   [1] {ECO:0000313|EMBL:OVE85743.1, ECO:0000313|Proteomes:UP000196084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3597 {ECO:0000313|EMBL:OVE85743.1,
RC   ECO:0000313|Proteomes:UP000196084};
RA   Zhao B.;
RT   "Natronthermophilus aegyptiacus gen. nov.,sp. nov., an aerobic, extremely
RT   halophilic alkalithermophilic archaeon isolated from the athalassohaline
RT   Wadi An Natrun, Egypt.";
RL   Submitted (FEB-2017) 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:OVE85743.1}.
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DR   EMBL; MWPH01000001; OVE85743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A202EBT1; -.
DR   OrthoDB; 10363at2157; -.
DR   Proteomes; UP000196084; 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:UP000196084}.
FT   DOMAIN          2..123
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          164..259
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          265..371
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          416..461
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   470 AA;  50028 MW;  B530B23F54D96B2E CRC64;
     MTLFGTAGIR GPVTEITPAL ALEVGQAAGE PGETFVVGRD GRETGPALAA AMEAGLESAG
     ASVVRIGQVP TPTLAFASRG RRGVMLTASH NPPEDNGIKL FADGVEYDRD AERAIEESIA
     SDDTDAVSWD DWGDSSRMDV LETYRKLVID YIGDELVDGT DASEPLAGFS IAVDCGNGMG
     SVATPHVLER LGAEVVALNA TVDGHFPARE SKPTPKTLRE FSAFLEEQDP HAVSDSEPRF
     DLGLAHDGDA DRLVVLGPDG EVIHEDTILA VVAEHYVATS EAADPVVVTT PNASARIDER
     VREAGGRVER VRLGALHEGI ARERAQGDDD TEVVFAAEPW KHIHTAFGGW IDGVVSAAAV
     ATLVADTGDT AALREPVTER PYRKISVDCP DDAKSDVMET LETALPETFS DTTVDTDYGV
     RLEFDDASWI LVRPSGTEPY VRIYAESDEV DDLVDEASDV VESTVADVSE
//