GenomeNet

Database: UniProt
Entry: J4WXX2_9GAMM
LinkDB: J4WXX2_9GAMM
Original site: J4WXX2_9GAMM 
ID   J4WXX2_9GAMM            Unreviewed;       451 AA.
AC   J4WXX2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   ORFNames=NT02SARS_1639 {ECO:0000313|EMBL:EJP72765.1};
OS   SAR86 cluster bacterium SAR86B.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX   NCBI_TaxID=1123867 {ECO:0000313|EMBL:EJP72765.1, ECO:0000313|Proteomes:UP000010116};
RN   [1] {ECO:0000313|EMBL:EJP72765.1, ECO:0000313|Proteomes:UP000010116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA   Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA   Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA   Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT   "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT   lineage.";
RL   ISME J. 6:1186-1199(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC         Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC         EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JH611188; EJP72765.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4WXX2; -.
DR   HOGENOM; CLU_016950_9_1_6; -.
DR   Proteomes; UP000010116; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010116}.
FT   DOMAIN          6..124
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          150..248
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          253..363
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          367..439
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   451 AA;  49913 MW;  3423B8DD7F066238 CRC64;
     MISESIFREN DIRGTYPEEL NEIVIKDIAK GIAKKCLQEG VSSIVVGRDG RLSGESLLKN
     FCDAISKYGI DVNNIGLATS PMLYFAAKKE ESRSGIMITG SHNPKNYNGI KMVINDASVS
     GSEILSLINN NENLESSSKG NINFCNIKEM YVREILENIN TDLSKLKVVI DSGNGAAGVV
     APELFKRLGC EVIELYSEVD GNFPNHHPDP GKLENLEDII SAVKNENADI GFAFDGDGDR
     VGLITNHGEM IFPDKQMMLF SKDVLNDRKG SIVFDVKCSN HLSNLISKNG GTPIMAPTGH
     FHIKKSIKKH NALLGGEMSG HIFFNDKWYG FDDGPYAAVR AAEILAKSNR SISDIFEEFP
     KSYSTPELNI SVTDENKFEI IEKFMTNSNI DGDKILIDGL RVNFDDGWGL LRASNTTPKL
     VLRFEGDTED SMNKIQNKFI SDYLAFVLRL I
//
DBGET integrated database retrieval system