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
//