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Database: UniProt
Entry: A4FNU1_SACEN
LinkDB: A4FNU1_SACEN
Original site: A4FNU1_SACEN 
ID   A4FNU1_SACEN            Unreviewed;       552 AA.
AC   A4FNU1;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:CAM05716.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:CAM05716.1};
GN   Name=pmmB {ECO:0000313|EMBL:CAM05716.1};
GN   OrderedLocusNames=SACE_6548 {ECO:0000313|EMBL:CAM05716.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM05716.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAM05716.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAM05716.1; -; Genomic_DNA.
DR   RefSeq; WP_009945069.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FNU1; -.
DR   STRING; 405948.SACE_6548; -.
DR   KEGG; sen:SACE_6548; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_2_11; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000006728; Chromosome.
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; cd05799; PGM2; 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; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR   PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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, ECO:0000313|EMBL:CAM05716.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN          55..190
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          211..308
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          321..435
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          479..522
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   552 AA;  58014 MW;  26704D3F6DFD1BF7 CRC64;
     MSGLDPQVRE AAERWVAGDV DARARDELLE LLGAADAGSA DAATELADRM SGMPTFGTAG
     LRGPVRAGAN GMNRAVVVRT TAGVAEWLRE RGHGGGIVVV GRDARHGSED FAADAAGVLA
     AAGFDVRVLP APLPTPVLAF ATRALDAVAG IQITASHNPP QDNGYKLYLR GGVHLVGPAD
     TEIEEAIART PDAASVPRSQ DYSVHHSALE DYLARVAELS KGSPRPLRVA ATALHGVGAR
     PLREALHRAG FDDVHLVASQ SEPDPDFPTV GFPNPEEPGA TDALLALAAE IEADLAIALD
     PDADRCALGI REDGRWRMLR GDETGVLLAQ HILSALDRQA HPDPLVATTI VSSTMLRSIA
     QEFRARYDET LTGFKWLVRA GDGAGTGLVY AYEEALGHCV DPEWVRDKDG ISTAVLACDL
     AAHVAADGRS IAGLLDALAI SHGVHQTGQV SVRVTDLGVI AETMRRLRRQ PPAELAGSPV
     EVQDLLPETD ALVVTGAGGL RVVIRPSGTE PKLKCYLQVV EQVTCGTIGT AKREAARRLS
     ELSTAVTELV AS
//
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