ID   I0EL77_HELC0            Unreviewed;       458 AA.
AC   I0EL77;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AFI03696.1};
GN   OrderedLocusNames=HCW_02055 {ECO:0000313|EMBL:AFI03696.1};
OS   Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI03696.1, ECO:0000313|Proteomes:UP000005010};
RN   [1] {ECO:0000313|Proteomes:UP000005010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA   Kersulyte D., Berg D.E.;
RT   "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL   Submitted (APR-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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; CP003479; AFI03696.1; -; Genomic_DNA.
DR   RefSeq; WP_014660568.1; NC_017737.1.
DR   AlphaFoldDB; I0EL77; -.
DR   STRING; 182217.HCW_02055; -.
DR   KEGG; hce:HCW_02055; -.
DR   PATRIC; fig|182217.3.peg.427; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_7; -.
DR   Proteomes; UP000005010; Chromosome.
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   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; IPR016066; A-D-PHexomutase_CS.
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.
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          5..129
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          155..250
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          257..365
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          377..456
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   458 AA;  51653 MW;  79E28310B761BDE3 CRC64;
     MDTSIFREYD IRGIYPKTLD ENTAFSIGVE LGKIMQQYSK GVFVGYDARV HGKKLFEALS
     AGLQQEGLKV YDLGLIPTPV AYFATFNEID NIQCPNSIMI TGSHNPKVYN GFKITLNNNP
     FYGKDIQALK DTLLNTTHEV KPLKEMPLKV NALEAYHNYL INDFKHLKDF KHKIALDFGN
     GVGALGLEPI LKALNIDFNS LYSEPNGNFP NHHPDPSVAK NLQDLQTHMQ ENAISIGFAF
     DGDADRIAML GANHIYTGDE LAILFAKHLY NQGITPFVIG EVKCSQVMYN TINSFGKTLM
     YKTGHSNLKV KLKETNAHFA AEMSGHIFFK ERYFGYDDAL YAALRALELM LKEDPSDLEN
     TIKNLPYSYT TPEEKILVSE EEKFEVIQNL QNKLQNVPDN FPRIKEIISI DGVRVVFEHG
     FGLIRASNTT PCLVTRFEGK DEKTALEYKK ALLGLLEK
//