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Database: UniProt
Entry: B9D421_CAMRE
LinkDB: B9D421_CAMRE
Original site: B9D421_CAMRE 
ID   B9D421_CAMRE            Unreviewed;       466 AA.
AC   B9D421;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II {ECO:0000313|EMBL:EEF13243.1};
DE            EC=5.4.2.2 {ECO:0000313|EMBL:EEF13243.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:EEF13243.1};
GN   ORFNames=CAMRE0001_2593 {ECO:0000313|EMBL:EEF13243.1};
OS   Campylobacter rectus RM3267.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF13243.1, ECO:0000313|Proteomes:UP000003082};
RN   [1] {ECO:0000313|EMBL:EEF13243.1, ECO:0000313|Proteomes:UP000003082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM3267 {ECO:0000313|EMBL:EEF13243.1,
RC   ECO:0000313|Proteomes:UP000003082};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (AUG-2008) 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}.
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:EEF13243.1}.
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DR   EMBL; ACFU01000024; EEF13243.1; -; Genomic_DNA.
DR   RefSeq; WP_002945113.1; NZ_ACFU01000024.1.
DR   AlphaFoldDB; B9D421; -.
DR   STRING; 553218.CAMRE0001_2593; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000003082; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 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   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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EEF13243.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          4..113
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..251
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          256..348
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          366..459
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   466 AA;  51931 MW;  87FEA1CFB75291A6 CRC64;
     MIDEIFREYD IRGVFERDLN EASVKAIGLN LGREMLRRGA KNVSVGFDAR LSAGEIFNRL
     VSGLNLSGIK VYDIGLLPTP IGYFSVFADK FDANIMITGS HNPKEYNGFK ITIFKDSYFG
     EDLQKLKTAV LDDIAAKTQI PDDFRAEKFD VATPYKNFLI EQFAHLKALP LKIVIDCANG
     AVGAVLPEIC EALKLNAQIL YPRPDGNFPN HHPDPSEEKN LSDLKAALKG EFDIGFGFDG
     DGDRIAVLTK KRNIKGDELA YLYSLAMKNP RVLGEVKCSQ NMYDEIDAHG GKSFMGKTGH
     SNIKKAMKEL NIDMAAEVSG HIFFKERYFG FDDAIYAMFR ALELVAKGFS LDGELGKLPK
     VFSTDEIKVK TTDTQKFKLV AKLKEVLVEI YEKGDAQNLL AGLGKIAQII DIDGVRVKFE
     DGSWALVRAS NTTPVIVTRF ETKDQNLLAR LQETFLNLVE NLKQKA
//
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