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Database: UniProt
Entry: A0A372NXQ4_9SPHI
LinkDB: A0A372NXQ4_9SPHI
Original site: A0A372NXQ4_9SPHI 
ID   A0A372NXQ4_9SPHI        Unreviewed;       470 AA.
AC   A0A372NXQ4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase family protein {ECO:0000313|EMBL:RFZ94449.1};
GN   ORFNames=D0C36_02545 {ECO:0000313|EMBL:RFZ94449.1};
OS   Mucilaginibacter conchicola.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=2303333 {ECO:0000313|EMBL:RFZ94449.1, ECO:0000313|Proteomes:UP000264217};
RN   [1] {ECO:0000313|EMBL:RFZ94449.1, ECO:0000313|Proteomes:UP000264217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYSH2 {ECO:0000313|EMBL:RFZ94449.1,
RC   ECO:0000313|Proteomes:UP000264217};
RA   Seo T.;
RT   "Mucilaginibacter sp. MYSH2.";
RL   Submitted (AUG-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:RFZ94449.1}.
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DR   EMBL; QWDC01000001; RFZ94449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372NXQ4; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000264217; Unassembled WGS sequence.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; 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   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   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}.
FT   DOMAIN          4..135
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          162..260
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          264..376
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          417..464
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   470 AA;  52347 MW;  A78DA8DFE2301985 CRC64;
     MIKIKFGTDG WRAIIADDFT LENVKRVAYA TALWLKDNFE NPSALVGCDP RFAGPMFADA
     TTCVLASQGI KVHRAENLFV STPMISLGTV RTGSSAGIII TASHNPPAYN GYKIKAFYGG
     PATPDDIEKV ENQIPDTLDL KLKTVADYVT DGLVEYINLE DMYVEHAEKN FDIPAIRDSG
     LQWAYDAMYG AGQNVMRRLF PDITFLHADY NPGFDGQAPE PIQRNLQEFE QLIKLSEGEI
     ASGLVTDGDA DRIGLYDGDG NFVDSHHILL LLIHYMHKVK GENGEVYSTF SCTSKIQKLC
     DAYGLNNTVT KIGFKYICDL IVNSGKQFMV GGEESGGIAV NGHIPERDGV WIGLMIWEFM
     AKTGRSLKDL VQEIYDVVGK FAVERYDLHV TEEKKQEIIS NSKNGKYETF GSLKVVRTED
     LDGFKFFFEN ETWVMIRPSG TEPVLRVYAE APTTAESFKI LDTVKAELLK
//
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