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Database: UniProt
Entry: H6RGF5_9BACT
LinkDB: H6RGF5_9BACT
Original site: H6RGF5_9BACT 
ID   H6RGF5_9BACT            Unreviewed;       732 AA.
AC   H6RGF5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase family protein {ECO:0000313|EMBL:CCG00116.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:CCG00116.1};
GN   ORFNames=VIS_S3CKB90001 {ECO:0000313|EMBL:CCG00116.1};
OS   uncultured Flavobacteriia bacterium.
OC   Bacteria; Bacteroidota; Flavobacteriia; environmental samples.
OX   NCBI_TaxID=212695 {ECO:0000313|EMBL:CCG00116.1};
RN   [1] {ECO:0000313|EMBL:CCG00116.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gomez-Pereira PR, Schuler M, Fuchs BM, Bennke C, Teeling H, Waldmann J,
RA   Richter M, Barbe V, Bataille E, Glockner FO, Amann R.;
RT   "Genomic content of uncultured Bacteroidetes from contrasting oceanic
RT   provinces in the North Atlantic Ocean.";
RL   Environ. Microbiol. 14:52-66(2012).
RN   [2] {ECO:0000313|EMBL:CCG00116.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope - CEA;
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; FO117599; CCG00116.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6RGF5; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05799; PGM2; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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:CCG00116.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          5..144
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   DOMAIN          192..332
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          360..465
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          474..585
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          670..702
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   732 AA;  79568 MW;  2FCEE5B68E05DB8D CRC64;
     MKKGGGRYHI VRTSWLYDNV GVNFFTTMVK LGQERSKIKV VYDQRGTPTY AGSLSDALRM
     LVLKGGDVKS GVLHFSDEGV TCWASFARAI FEELEMDVEV VGITTSEYPT HALRPANSHL
     GGKQFRTLLN LEKRTWKESL KMCVGSELER VKRRAKVWSK APYDKETRDT VGMWLSENKE
     DVLTEAFHKD ITFGTGGMRG ICGPGTNRIN AAVISGATQG LVNYIKKTKQ HSSTPLKVAI
     AYDCRHQSYE FAEVTARVLA GNGIQALLYP ELRPTPQLSW TVRNLGCVAG VVVTASHNPP
     EYNGYKVYWE DGGQIVSPHD SAIIGEVRKI KSLSEVKIAS REIASEDLIT LLGPEQDEGY
     LNAILKLRRS VSLEENGSAS CLVFTGLHGT GSVSVPPALR AFGFSNIHEV KSQSLPDGNF
     PTVSSPNPEE GQALAEAISL GEKLGATLVM GTDPDADRVG VAVTNGDGGF QLLNGNETGA
     LLFDYVIRCG RDNGDSYDSS DFVASTVVTS PLLSAIGESY GLGVRTTLTG FKHIAAAITE
     EEKGMNGRNF IVGAEESYGY LIKDTARDKD AVAACCVLSE LAHSLEENGT TMLARLESIH
     RKHGLYQEGL VSIVKMGREG ANEISEMMSR FRSSTPGMLA GEKVVGLLDF ETQKNHDLIS
     SKVKNIDLPK SNVLQFVTEK GSRITVRPSG TEPKIKFYVS VNTTLQENDD YLEKKTALTS
     QIAALFHAVG AA
//
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