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Database: UniProt
Entry: A0A5C6RUD0_9FLAO
LinkDB: A0A5C6RUD0_9FLAO
Original site: A0A5C6RUD0_9FLAO 
ID   A0A5C6RUD0_9FLAO        Unreviewed;       470 AA.
AC   A0A5C6RUD0;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   28-JAN-2026, entry version 16.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase family protein {ECO:0000313|EMBL:TXB66096.1};
GN   ORFNames=FRY74_05870 {ECO:0000313|EMBL:TXB66096.1};
OS   Vicingus serpentipes.
OC   Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Vicingaceae; Vicingus.
OX   NCBI_TaxID=1926625 {ECO:0000313|EMBL:TXB66096.1, ECO:0000313|Proteomes:UP000321721};
RN   [1] {ECO:0000313|EMBL:TXB66096.1, ECO:0000313|Proteomes:UP000321721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 15042 {ECO:0000313|EMBL:TXB66096.1,
RC   ECO:0000313|Proteomes:UP000321721};
RA   Bowman J.P.;
RT   "Genome of Vicingus serpentipes NCIMB 15042.";
RL   Submitted (AUG-2019) 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:TXB66096.1}.
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DR   EMBL; VOOS01000002; TXB66096.1; -; Genomic_DNA.
DR   RefSeq; WP_147099547.1; NZ_VOOS01000002.1.
DR   AlphaFoldDB; A0A5C6RUD0; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000321721; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:TreeGrafter.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:TreeGrafter.
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; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2B-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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
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:UP000321721}.
FT   DOMAIN          4..137
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          163..261
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          265..375
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          407..459
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   470 AA;  52827 MW;  B86BF2269A8C4812 CRC64;
     MAQIKFGTDG WRAIIAKDYT VDNVARVALA TATWLKHNFK KPSVVIGHDC RFAGEMFAET
     TAKVLANAGI KVYIAKDFVT TPMVSLGTLR QKASLGVVIT ASHNPPSYNG FKLKGSFGGP
     LLPKEIQEVE DLIPEENNIN LEILNFEKFI ENGIIEYIDL ETMYVEHVEA NFDMNAIRNS
     DMNFAYDAMY GAGQNVMRRL LPEIDFLHCD YNPGFEGVAP EPIHRNLMEF SEMIKLAEGQ
     INCGLATDGD ADRIGLYDSN GEFVDSHHII LLLIKYLVEE KKMTGKVVNA FSVTPKVKKM
     CDHYGLDYQV TQIGFKYIAG VMVNEDVLLG GEESGGIAVK GHIPERDGIW MGLIIWEYMV
     KSGKTLEELI EEMYQIVGGF KFERIDLKLK EADKLRIMEN CKNDVYKAFG DLKVNEVQTI
     DGFKYFFDND EWVMIRPSGT EPVLRTYAEA ATTEAAFKIL EKTHATINKA
//
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