ID A0A840UVD7_9FIRM Unreviewed; 450 AA.
AC A0A840UVD7;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:MBB5336784.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:MBB5336784.1};
GN ORFNames=HNR32_001939 {ECO:0000313|EMBL:MBB5336784.1};
OS Pectinatus brassicae.
OC Bacteria; Bacillati; Bacillota; Negativicutes; Selenomonadales;
OC Selenomonadaceae; Pectinatus.
OX NCBI_TaxID=862415 {ECO:0000313|EMBL:MBB5336784.1, ECO:0000313|Proteomes:UP000559117};
RN [1] {ECO:0000313|EMBL:MBB5336784.1, ECO:0000313|Proteomes:UP000559117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24661 {ECO:0000313|EMBL:MBB5336784.1,
RC ECO:0000313|Proteomes:UP000559117};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBB5336784.1}.
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DR EMBL; JACHFH010000024; MBB5336784.1; -; Genomic_DNA.
DR RefSeq; WP_183862035.1; NZ_JACHFH010000024.1.
DR AlphaFoldDB; A0A840UVD7; -.
DR Proteomes; UP000559117; 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:MBB5336784.1};
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:UP000559117}.
FT DOMAIN 6..131
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 258..368
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 373..438
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 450 AA; 50046 MW; 24BB3C99D1AA71FC CRC64;
MELKRTAFKA YDIRGKYPEE VNEELAYRIG RVFAKSFAAK KVVVGHDIRL SGPDIRDALV
QGLTDMGCDV IDIGQCGTEM IYFATYFWQL DGGIMITASH NPKDYNGMKL VREGARPISA
DTGLKDIENK AIAGELGEIA ATKGSVEQKD IMADYVDHIL AYVDKKDLKP LKIVVNAGNG
AAGPILDEME KALPFEFIKI NNEPDGNFPN GVPNPILLEN RVATAKAVRE NNADVGIAWD
GDFDRCFIFD EKGDMIEGYY IVGFLAKAFL DKNPGAKIIY DPRLIWNTIE IVEEAGGIPV
MCKSGHAFIK EMMRKVDAVY GGEMSAHNYF REFTFCDSGM ITWLLVLELV SKANQPLSKM
LAERMQRYPI SGEINSTVKD GAAVMLKMEE LYGPKGQVDK TDGLSVAFAD WRFNLRISNT
EPVIRLNVEA RGDKELLDAK TKELLEIIRA
//
