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
//