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Database: UniProt
Entry: A0A0D6BAA0_RHOSU
LinkDB: A0A0D6BAA0_RHOSU
Original site: A0A0D6BAA0_RHOSU 
ID   A0A0D6BAA0_RHOSU        Unreviewed;       474 AA.
AC   A0A0D6BAA0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:BAQ71689.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:BAQ71689.1};
GN   Name=manB {ECO:0000313|EMBL:BAQ71689.1};
GN   ORFNames=NHU_04576 {ECO:0000313|EMBL:BAQ71689.1};
OS   Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OG   Plasmid Plasmid3 DNA {ECO:0000313|Proteomes:UP000064912}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ71689.1, ECO:0000313|Proteomes:UP000064912};
RN   [1] {ECO:0000313|EMBL:BAQ71689.1, ECO:0000313|Proteomes:UP000064912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ71689.1,
RC   ECO:0000313|Proteomes:UP000064912};
RC   PLASMID=Plasmid Plasmid3 DNA {ECO:0000313|Proteomes:UP000064912};
RA   Nagao N.;
RT   "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AP014803; BAQ71689.1; -; Genomic_DNA.
DR   RefSeq; WP_060836800.1; NZ_AP014803.1.
DR   AlphaFoldDB; A0A0D6BAA0; -.
DR   KEGG; rsu:NHU_04576; -.
DR   PATRIC; fig|35806.4.peg.4694; -.
DR   Proteomes; UP000064912; Plasmid Plasmid3 DNA.
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; cd03088; ManB; 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   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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:BAQ71689.1};
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   Plasmid {ECO:0000313|EMBL:BAQ71689.1}.
FT   DOMAIN          4..126
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          150..247
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          252..369
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          402..455
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   474 AA;  48127 MW;  9131E8429BBC7CC5 CRC64;
     MAPKFGTSGL RGLVSELTPD LVGAYVRAFL MACPAGPRVL VGRDLRASSP RIAEDAIAAI
     RAAGREAVDC GALPTPALAL VAMGQGAAAI MVTGSHIPAD RNGLKFYLPS GEISKADEAA
     IGQALERPVA APAPAAGQGA RSFAPEAGAA YVARYVQAFG DAALAGLRVG VYQHSSVARE
     TLVEILGALG AEPVPLAASD SFVPVDTEAV DAGTRAMLAE WCAGQGLDAL VSTDGDADRP
     MLTDAAGRVV PGDILGALTA RALGAEAVCT PVSSNSLVTR LPEFETVRLT RIGSPFVIAA
     MEEILAADPA ARVAGFEANG GFLLGFAARG PAGPLAPLMT RDAMLPLVTV LAAARAAGSG
     VAGVVAALPA RHTAADRLQQ VAPEAAVALL ARLDASARAR DAFFAPLGRE AGCDRTDGLR
     VSFASGEILH LRPSGNAPEF RVYAEADSPE RAAAVLKLGL ERVAAALADR DAQE
//
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