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Database: UniProt
Entry: K1ZWA7_9BACT
LinkDB: K1ZWA7_9BACT
Original site: K1ZWA7_9BACT 
ID   K1ZWA7_9BACT            Unreviewed;       286 AA.
AC   K1ZWA7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Phosphomannomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACD_64C00271G0001 {ECO:0000313|EMBL:EKD48513.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD48513.1};
RN   [1] {ECO:0000313|EMBL:EKD48513.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EKD48513.1}.
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DR   EMBL; AMFJ01027031; EKD48513.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1ZWA7; -.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 2.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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   PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
PE   4: Predicted;
FT   DOMAIN          1..66
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          75..184
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          195..264
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   286 AA;  31970 MW;  3C1A2B0C91F314EE CRC64;
     MLPELIKQME WKNVTLLYED VDGTFPNHEA DPTVEKNMLA VKDALTTQDI TVGIGLDGDC
     DRMTPMTKQA KLVSGDQLLA LFAQTVLSEH PGAGIVFDIK SSLGLIELLE QWGADPIMSP
     SGHSIIKDMM SKHGALLGGE ISCHFFFKDR YFGYDDGIYA AMRLLELLHT SGTSLTELLT
     IFPKKYSSQE FRLFCPDEKK QEVIKAIKKE ISHRDNVKIS TIDGVRAVFP FGWGIVRASN
     TQAALSMRFE SDTQTGLKTV MNLFYTLLEP YLEKKDVDLL HTKDAA
//
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