ID   B5YHC5_THEYD            Unreviewed;       459 AA.
AC   B5YHC5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:ACI20231.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:ACI20231.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ACI20231.1};
GN   OrderedLocusNames=THEYE_A0095 {ECO:0000313|EMBL:ACI20231.1};
OS   Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC   Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC   Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX   NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI20231.1, ECO:0000313|Proteomes:UP000000718};
RN   [1] {ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT   ATCC 51303 / DSM 11347 / YP87.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI20231.1, ECO:0000313|Proteomes:UP000000718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51303 / DSM 11347 / YP87
RC   {ECO:0000313|Proteomes:UP000000718};
RX   PubMed=25635016;
RA   Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA   Robb F.T., Ward N.L., Eisen J.A.;
RT   "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT   Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL   Genome Announc. 3:0-0(2015).
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; CP001147; ACI20231.1; -; Genomic_DNA.
DR   RefSeq; WP_012544969.1; NC_011296.1.
DR   RefSeq; YP_002247947.1; NC_011296.1.
DR   AlphaFoldDB; B5YHC5; -.
DR   STRING; 289376.THEYE_A0095; -.
DR   EnsemblBacteria; ACI20231; ACI20231; THEYE_A0095.
DR   KEGG; tye:THEYE_A0095; -.
DR   PATRIC; fig|289376.4.peg.93; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_0; -.
DR   InParanoid; B5YHC5; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000000718; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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:ACI20231.1};
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:UP000000718}.
FT   DOMAIN          4..138
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..252
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          256..356
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          374..445
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   459 AA;  51982 MW;  F0774748F0E1DC8A CRC64;
     MEDRIFREYD IRGIYGEDLT EEISYLIGKA FVSLVFKELK RMPRKISVGM DARFSSETLK
     KELLKGITEC GVDVIDIGLC PTPLQYFSLF TLPVDAGIMI TGSHNPPEFN GFKLSIGKET
     IYGEKIRRLK KIIEKKDFIN FNKTGKIEKY NITDDYINYM LSGFTSFEGI KVVVDSGNGT
     AGLVAPVILK KLGAEVYELY SEPDGRFPNH HPDPVVLENM EDLIQTVINK KAHLGIGFDG
     DADRIGVIDE SGDVVWGDRL MIIFAKDILE ENKGAKIIGE VKCSKVMYEE IAKAGGIPVM
     WKTGHSLIKK KMKEEGALLA GEMSGHIFFS DKYFGFDDAI YASLRLVEIV KKAGKPYGIK
     KLLCGVKTMQ STPEIRIDCI DEKKFMIVEK IKDYFQKFEC NFIDGVRINF KKGWALIRAS
     NTQPALVLRF EAETEDDLEE IKSIVHQKLF EVFQFFKIL
//