ID Q0AV09_SYNWW Unreviewed; 449 AA.
AC Q0AV09;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ABI69445.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:ABI69445.1};
GN OrderedLocusNames=Swol_2154 {ECO:0000313|EMBL:ABI69445.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI69445.1, ECO:0000313|Proteomes:UP000001968};
RN [1] {ECO:0000313|Proteomes:UP000001968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI69445.1; -; Genomic_DNA.
DR RefSeq; WP_011641536.1; NC_008346.1.
DR AlphaFoldDB; Q0AV09; -.
DR STRING; 335541.Swol_2154; -.
DR KEGG; swo:Swol_2154; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_9; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001968; 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; 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, ECO:0000313|EMBL:ABI69445.1};
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:UP000001968}.
FT DOMAIN 6..133
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..251
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 256..365
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 371..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 449 AA; 50049 MW; 1BF571B7EF681CA7 CRC64;
MINQSIFRMY DIRGRVGTDL DEVAVRAIAA AFGKYVQERG RDKIIVGRDN RFSSPRFREL
VVETLLLSGL DVVDIGEVIT PMFYFASRHL DIDAGMMITA SHNPGEDNGF KLLLGNSTIY
GEDILKIAEL AEAGGFTSST NKGNLSFYDI SPAYQQDIMK RIKLGERKLK VVVDCGNGTA
GFIAPRLFRE LGCEVIELYC DSDPSFPNHH PDPVKVENCQ DLIQVVKAER ADLGIGFDGD
GDRLGVVDTE GNIIWGDMLM ILFWREILPS YPGTDCIVEV KCSQSLIDEI NRLGGKPIIY
KTGHSLIKAR MKEIGAVFTG EMSGHMFFAD EYYGYDDALY AAARLLRILS HSEQSLNELL
ADVPRYHATP ELRVKSSDSE KFAVVERVLS HYRNHHEVID IDGARILFPG GWGLVRASNT
GPELIVRCEA GTPEELERIK AELFAFLEV
//
