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
//