ID A0A3G8ZVS7_9ACTN Unreviewed; 558 AA.
AC A0A3G8ZVS7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE SubName: Full=Phospho-sugar mutase {ECO:0000313|EMBL:AZI58564.1};
GN ORFNames=EH165_10915 {ECO:0000313|EMBL:AZI58564.1};
OS Nakamurella antarctica.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Nakamurellales;
OC Nakamurellaceae; Nakamurella.
OX NCBI_TaxID=1902245 {ECO:0000313|EMBL:AZI58564.1, ECO:0000313|Proteomes:UP000268084};
RN [1] {ECO:0000313|EMBL:AZI58564.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI58564.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Da X.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AZI58564.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI58564.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Peng F.;
RT "Nakamurella antarcticus sp. nov., isolated from Antarctica South Shetland
RT Islands soil.";
RL Submitted (DEC-2018) 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; CP034170; AZI58564.1; -; Genomic_DNA.
DR RefSeq; WP_124799473.1; NZ_CP034170.1.
DR AlphaFoldDB; A0A3G8ZVS7; -.
DR KEGG; nak:EH165_10915; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000268084; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:TreeGrafter.
DR CDD; cd05799; PGM2; 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; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2B-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000268084}.
FT DOMAIN 57..191
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 215..311
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 488..522
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 558 AA; 57633 MW; EDCA071B1EE18CA5 CRC64;
MSATALDGDL RRAVVRWIAD DPSPADAAEL KGILADAMAG DAAAIGELTD RMSAPLAFGT
AGLRGPLRAG PAGMNLAVVR RAAAGIAAYL RNVGSAGESV VIGYDARHRS AEFAHDAAGV
LAAAGFRVLL APSALPTPLT AFGVRSLGAV AGLMVTASHN PPNDNGLKVY LAGGTQLVWP
ADVQIEAAIA AAPAGVAIDA TGQAQPWPDS LIGDYLDRAA AVATGGAKSL RIAATPMHGV
GGETLVKALY QAGFSDVHMV AEQAVPDPDF PTVAFPNPEE PGAADLLLAL ATAIDADLAI
ANDPDADRCA IGIKDVNGIW RMLTGNETGA LLGDRVLRGL DRGAHPDPLV ATTIVSSAML
KSIAAQHDVR FDETLTGFKW IVRAGDGDGT GLVFGFEEAL GLCVDPTVVR DKDGISAAVL
ACDLAATLKA GGRHITDALD DLARQHGLHA TDQLSFRVAD LSLITDGMAR LRGNIPIELL
GETVLTTKDL LPQTDAVVLH TERVRVVIRP SGTEPKLKCY LEIITPVGVD DDLTAIREAS
AGQLTALKSE LREVLQLG
//
