ID E3BPT5_9VIBR Unreviewed; 547 AA.
AC E3BPT5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:EFP95003.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:EFP95003.1};
GN ORFNames=VIBC2010_13121 {ECO:0000313|EMBL:EFP95003.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP95003.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP95003.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP95003.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EFP95003.1}.
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DR EMBL; AEIU01000110; EFP95003.1; -; Genomic_DNA.
DR RefSeq; WP_009603196.1; NZ_AEIU01000110.1.
DR AlphaFoldDB; E3BPT5; -.
DR STRING; 796620.VIBC2010_13121; -.
DR eggNOG; COG0033; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000002943; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR045244; PGM.
DR InterPro; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
DR PANTHER; PTHR22573:SF57; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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 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:EFP95003.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943}.
FT DOMAIN 41..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 320..435
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 489..537
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 547 AA; 59937 MW; 3ABD2E81AEA6A91A CRC64;
MATHSRAGLR AEQKDLPNIP VLVSNYFLLE PDPLNPSHSV VFGTSGHRGS SDKSSFNQYH
IWAIAQAIAE IRKKEGINGP LFVGKDTHAL SEPAFISVVE VLIANGVEVR LQENNGYTPT
PSISHAILEH NKCEDVKADG IVITPSHNPP QDGGIKYNPP HGGPADDRLT REIQQRANEI
IQNGMKPVER LAFSQARLSP LFVELDLVTP YVDDLVNVID IEAIKKANLK FGVDPLGGSG
VEYWRQIGRK YDLDLTLVSE SIDPSFQFMP LDKDGVIRMD CSSPYAMAGL LALKDQYDLA
FGNDPDFDRH GIVTPSGLMN PNHFLAVCID YLFKHRDWHQ EINVGKTLVS SALIDRVVSD
LGRNLCEVPV GFKWFVDGLY NGQIGFGGEE SAGASFLRKD GTPWSTDKDG IILCLLAAEI
TAVTGLNPQE YYQTLAAKHG ESYYSRLQAT ATGPQKEILK ALNPEMVESD SLAGETILQR
LTHASGNGAA IGGLKVSTKN GWFAARPSGT EDIYKIYCES FISAEHLRLI EQQAQEIVNQ
VFAKAGL
//
