ID D8JZ66_HYPDA Unreviewed; 501 AA.
AC D8JZ66;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II {ECO:0000313|EMBL:ADJ23668.1};
GN OrderedLocusNames=Hden_1865 {ECO:0000313|EMBL:ADJ23668.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ23668.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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}.
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DR EMBL; CP002083; ADJ23668.1; -; Genomic_DNA.
DR RefSeq; WP_013215827.1; NC_014313.1.
DR AlphaFoldDB; D8JZ66; -.
DR STRING; 582899.Hden_1865; -.
DR KEGG; hdn:Hden_1865; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_5; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000002033; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002033}.
FT DOMAIN 26..157
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 175..272
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..390
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 419..486
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 501 AA; 55198 MW; D65EC042439374D2 CRC64;
MLPKPRADLK PNTADFERLP LVKPTGFREY DARWLFPEEI NLMGLNAVGL GMATLFTRRG
VPRRIVVGHD YRWYSGAVKQ ALMTGLLAGG CEVHDIGLAL SPMAYFAQFE LDVEGVAMVT
ASHNDNGWTG IKMGLSRPLT FGPDDMSELK SIVLNGDYET RTGGRYIFVH DMAERYVKSL
TNRPKLKRRL KVVAACGNGT AGAFAAEVLS AVGCEVVPLN TDLDHSFPNH NPNPEDMKML
HAVAAKVRET NADVGLAFDG DGDRCGVVAN DGHEIFADKV GVMLARDISS LHRNAKFVVD
VKSTGLFTTD PVLIANGATT TYWKTGHSYI KRFNFENKTL VGFEKSGHFF FNTPLGRGYD
DGLIAALAVC DMLDRNPDKS IADLRDALPK TWSSPTMSPH CDDEKKYDVV ERITEHYKRQ
KDSGGHIAGQ AIRDLITVNG VRVMLEDGTW GLVRASSNKP ELVVVVESPT SEANMKAIFK
DIDQQLSRFP EVGEYNQKIA V
//
