ID J0D351_HELPX Unreviewed; 458 AA.
AC J0D351;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Phosphohexosemutase {ECO:0000313|EMBL:EJB80338.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:EJB80338.1};
GN Name=algC {ECO:0000313|EMBL:EJB80338.1};
GN ORFNames=HPHPH6_1496 {ECO:0000313|EMBL:EJB80338.1};
OS Helicobacter pylori Hp H-6.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992061 {ECO:0000313|EMBL:EJB80338.1, ECO:0000313|Proteomes:UP000004177};
RN [1] {ECO:0000313|EMBL:EJB80338.1, ECO:0000313|Proteomes:UP000004177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp H-6 {ECO:0000313|EMBL:EJB80338.1,
RC ECO:0000313|Proteomes:UP000004177};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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:EJB80338.1}.
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DR EMBL; AKOZ01000007; EJB80338.1; -; Genomic_DNA.
DR AlphaFoldDB; J0D351; -.
DR PATRIC; fig|992061.3.peg.1467; -.
DR Proteomes; UP000004177; Unassembled WGS sequence.
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; 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, ECO:0000313|EMBL:EJB80338.1};
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..128
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 258..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 375..456
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 458 AA; 51763 MW; 7555EE4D079A8D29 CRC64;
MDISIFREYD IRGIYPTTLD ENTAFSIGVE LGKIMREYDK SVFVGHDARV HGRFLFEALS
AGLQSSSLKV YDLGLIPTPV AYFAAFNEIN GIQCPNSIMI TGSHNPKEYN GFKITLNQNP
FYGKDIQALK NTLLNAKHEI KPLKETPKKV NALEAYHRYL IKDFKHLKNL KYKIALDFGN
GVGALGLEPI LKALNIDFSS LYSDPDGNFP NHHPDPSEAK NLKDLEKHMR ENAILIGFAF
DGDADRIAML SSHHVYAGDE LAILFAKRLH AQGITPFVIG EVKCSQVMYN TINTFGKTLM
YKTGHSNLKI KLKETNAHFA AEMSGHIFFK ERYFGYDDAL YACLRALELL LEQSPSDLEN
TIKNLPYSYT TPEEKIAVSE EEKFEIIHNL QETLKNPPSH FPTIKEIISI DGVRVVFEHG
FGLIRASNTT PYLVSRFEGK DETTALEYKR ALLNLLEK
//
