ID A0A0G1LAV8_9BACT Unreviewed; 458 AA.
AC A0A0G1LAV8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=UW94_C0010G0009 {ECO:0000313|EMBL:KKT93015.1};
OS Parcubacteria group bacterium GW2011_GWA2_45_14.
OC Bacteria.
OX NCBI_TaxID=1618832 {ECO:0000313|EMBL:KKT93015.1, ECO:0000313|Proteomes:UP000034475};
RN [1] {ECO:0000313|EMBL:KKT93015.1, ECO:0000313|Proteomes:UP000034475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT93015.1}.
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DR EMBL; LCKH01000010; KKT93015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LAV8; -.
DR STRING; 1618832.UW94_C0010G0009; -.
DR PATRIC; fig|1618832.3.peg.934; -.
DR Proteomes; UP000034475; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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};
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}.
FT DOMAIN 21..145
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 165..261
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 266..370
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 379..453
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 458 AA; 50945 MW; 00DDDCFEA45E8465 CRC64;
MVDFINISNF IDIMFNASIY RSYDIRGIVP TELDKEECYH IGRAYAKFTG AKRVVVARDM
RPSGDEFEPE LVRGLTEGGV NVIRIGLATS PMFYFAVHFF GADGGVMVTA SHNPGQYNGL
KMTRAEAVPI AGDSGLMDIR DLAEKRDWEA VTQAGKTEDK QIKDEYVQMV TAGFSAEGLK
IVVDAGNGMS GYILKDVFER LGGEVVPLYW ELDGSFPNHE ADPLKEENLE DLKKVMKQEK
ADLGVAFDGD ADRVFFVTDQ GETVPGDITT AIIAKEVLAK HKGAPVLYDI RASWTTPDVI
KEAGGEPVMW KVGHSLIKAK MREVGAKFAG EVSGHFFFTP WFAESGMLAM GHVLTVVRRE
GKSLSEIVKP LLRYVKTPEI NYDVPDKEAA IARIKNQYSD ASRIFDFDGI RFEYEDWWAS
VRPSNTEPKL RLNMEAKTSE LLEKKKAEIE GLIKGDGK
//
