ID A0A0U1KT95_9FIRM Unreviewed; 453 AA.
AC A0A0U1KT95;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=SpAn4DRAFT_1444 {ECO:0000313|EMBL:CQR70475.1};
OS Sporomusa ovata.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=2378 {ECO:0000313|EMBL:CQR70475.1, ECO:0000313|Proteomes:UP000049855};
RN [1] {ECO:0000313|Proteomes:UP000049855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nijsse Bart;
RL Submitted (MAR-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; CTRP01000003; CQR70475.1; -; Genomic_DNA.
DR RefSeq; WP_021169209.1; NZ_CTRP01000003.1.
DR AlphaFoldDB; A0A0U1KT95; -.
DR Proteomes; UP000049855; Unassembled WGS sequence.
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; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; 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:CQR70475.1};
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:UP000049855}.
FT DOMAIN 6..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 155..255
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 260..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 375..450
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 453 AA; 50324 MW; A708E71A4FBA798F CRC64;
MEIKRAAFKA YDIRGKVPEE LNEAMAYRIG RAFVDIVAAK KVAVGNDIRL SGPAFKSAVI
KGLTEMGCDV VDIGLCGTEQ IYFATAHLKL DGGIMITASH NPKDYNGMKL VRAESRPISG
DTGLKELEEQ VVTGEFPPVS KNIIPGKVTC VDILKDYIEH LLTYVDKAAL KPLKVVVNAG
NGGAGAVIDA LEPYLPFEFI KVNHQPDGNF PNGVPNPLLI ENREVTAKAV RENGADVGIA
WDGDFDRCFL FDEKGDFIEG YYLVGFLAQA FLQRRPGSKI IYDPRLTWNT IELVEKAGGI
PVLSKSGHAF IKERMRKEDA VYGGEMSAHH YFKDFSYCDS GMIPWLLVLE ILCREGKPLS
VLMRERVACY PVSGEINSTV ADARAVIQQI EEKYTPGALK IERVDGLSVE YDKWRFNVRM
SNTEPVLRLN VESRCDVKLM EEKTRELLAL IRG
//
