ID   A0A495KSK0_9FLAO        Unreviewed;       466 AA.
AC   A0A495KSK0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:RKS03559.1};
GN   ORFNames=C8C84_3319 {ECO:0000313|EMBL:RKS03559.1};
OS   Flavobacterium sp. 102.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2135623 {ECO:0000313|EMBL:RKS03559.1, ECO:0000313|Proteomes:UP000270484};
RN   [1] {ECO:0000313|EMBL:RKS03559.1, ECO:0000313|Proteomes:UP000270484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=102 {ECO:0000313|EMBL:RKS03559.1,
RC   ECO:0000313|Proteomes:UP000270484};
RA   Chistoserdova L.;
RT   "Synthetic bacterial communities of pure cultures isolated from sediment of
RT   Lake Washington, USA.";
RL   Submitted (OCT-2018) 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:RKS03559.1}.
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DR   EMBL; RBKX01000001; RKS03559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495KSK0; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000270484; Unassembled WGS sequence.
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   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          8..142
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          173..263
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          270..376
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          400..461
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   466 AA;  50399 MW;  FE33A1E374BF714C CRC64;
     MTLIKSISGI RGTIGGNVGD NLTPVDAVKF ASAYGTFLKN NIQKDKLKVV IGRDARISGP
     MIHNLVVNTL IGLGIDVIDL GLSTTPTVEV AVPMEEADGG IILTASHNPK QWNALKLLNA
     KGEFLSGADG AKILEIAEAE AFDFSDVDSL GEITMNDAYM DIHIDEVLDL PLVDAEAVAK
     RKFKVVVDGV NSSGGIIIPK LLEQMGVECV KLYCEPNGHF PHNPEPLKEH LGDICKLVLE
     EKADFGIVVD PDVDRLAFIS NDGEMFGEEY TLVACADYVL SKTPGNTVSN MSSSRALRDI
     TEKYNGSYQA SAVGEVNVVE LMKASNAIIG GEGNGGIIYP ELHYGRDSLV GVALFLTHLA
     SLDMTVAELR ASYPQYYMSK NKIELTPQID VDAILLAMTE KYKNDRSTSS LSTIDGVKVD
     FADNWVHLRK SNTEPIIRIY TEAPTQEAAD QLALRIIDEI KAVAGI
//