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Database: UniProt
Entry: Q0BX82_HYPNA
LinkDB: Q0BX82_HYPNA
Original site: Q0BX82_HYPNA 
ID   Q0BX82_HYPNA            Unreviewed;       505 AA.
AC   Q0BX82;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Putative phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:ABI76835.1};
GN   OrderedLocusNames=HNE_3238 {ECO:0000313|EMBL:ABI76835.1};
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI76835.1, ECO:0000313|Proteomes:UP000001959};
RN   [1] {ECO:0000313|EMBL:ABI76835.1, ECO:0000313|Proteomes:UP000001959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI76835.1,
RC   ECO:0000313|Proteomes:UP000001959};
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI76835.1; -; Genomic_DNA.
DR   RefSeq; WP_011648207.1; NC_008358.1.
DR   AlphaFoldDB; Q0BX82; -.
DR   STRING; 228405.HNE_3238; -.
DR   KEGG; hne:HNE_3238; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_1_5; -.
DR   Proteomes; UP000001959; 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:UP000001959}.
FT   DOMAIN          41..161
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          182..279
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          285..392
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          436..488
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   505 AA;  54767 MW;  40C95C26ECC50BFE CRC64;
     MFPKPLADIA PNTLEFEVLP LVKPTGFREY DARWWFNGIG HAKPAELNLT GVQALGLGMA
     TLFHELGVKP TVVTGHDYRS ISQPIKNALT LGLMAGGCEV LDVGLALSPM VYWSQFELDA
     ACCAMVTASH NENGWTGVKM GADRPLTFGP DEMGRLKEIV MGGKFVTREG GTHRRIDGIR
     EKYIKAVVGD TKLTRKLKVV AACGNGTAGA FAGDVLRAIG ADVIEMDCNL DMTFPKYNPN
     PEDQEMLHAM AVTVKETGAD LALGFDGDGD RCGVVDNNGE EIYADKIGLM LARDLSKNFA
     NAKFVVDVKS TGLYKTDPVL KANGATVDYY KTGHSYIKRR TNELGALAGF EKSGHFFFRP
     PIGLGYDDGL IAAKAILEML DRNPGKTMAD LNGELGVAYT SLTMAAHCGD EVKYDVVDKM
     VAEYQGLDGT MILGRKVVEV NTVNGARVTL EDGSWVLVRA SSNKPELVVV VESMSSEADM
     KDLFHKEVKP RLGKHAEVGK YNQEI
//
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