ID A0A0G1NMG3_9BACT Unreviewed; 483 AA.
AC A0A0G1NMG3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:KKU21764.1};
DE Flags: Fragment;
GN ORFNames=UX33_C0022G0011 {ECO:0000313|EMBL:KKU21764.1};
OS Candidatus Azambacteria bacterium GW2011_GWC1_46_13.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1618619 {ECO:0000313|EMBL:KKU21764.1, ECO:0000313|Proteomes:UP000034569};
RN [1] {ECO:0000313|EMBL:KKU21764.1, ECO:0000313|Proteomes:UP000034569}
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}.
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:KKU21764.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCLU01000022; KKU21764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NMG3; -.
DR PATRIC; fig|1618619.3.peg.443; -.
DR Proteomes; UP000034569; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 1..85
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 127..199
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 205..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 318..385
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKU21764.1"
SQ SEQUENCE 483 AA; 54359 MW; B3336CA3F3F896A7 CRC64;
VVGSDARISS PGLKKALVRG ILEQGGKIID IGLATTPMFY FAVNKAKADG GAMVTASHNP
AKYNGLKFTL KQARPVGEET GLEEIKLLAL RAKFKAAAKK GTLKKKSLFK KYVNFMLRQI
KNIEMMAGLI LPHLFKRMKR IKIFPLYFKV DCGFPNHEAN PLKEDTLNDL KNLMRKKKVD
MGVAFDGDGD RVVFLTAEGR PARADFITAL LAGEYLKKYP KAKIAFGVNS SRVVREAIAE
KGGRPFVSRI GHSFFKEHLW KEGVVFGGEL SGHYYFRDFF NADSGIFTMM KVLKIVAQEK
KPLSELIKPF ERYFASGEIN FEVKDKFGII KNLEKKFSDG RVSKVDGLSV EYKDWWFNVR
SSNTEPLLRL NLEAKTKKML EEKKKMLTIL TAIIEGPFSV TLIKVTPVFE MRGNFLKLRS
GISKILISIK VIAPPWETIR TSPWSFPERI SRVMPVMTSL MNCVTRRCVA LSVSPFGNLT
FSG
//
