ID A0A0S8DFT3_9BACT Unreviewed; 581 AA.
AC A0A0S8DFT3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KPK34394.1};
GN ORFNames=AMK70_07550 {ECO:0000313|EMBL:KPK34394.1};
OS Nitrospira bacterium SG8_35_1.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704024 {ECO:0000313|EMBL:KPK34394.1, ECO:0000313|Proteomes:UP000052010};
RN [1] {ECO:0000313|EMBL:KPK34394.1, ECO:0000313|Proteomes:UP000052010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_1 {ECO:0000313|EMBL:KPK34394.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK34394.1}.
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; LJTK01000107; KPK34394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DFT3; -.
DR PATRIC; fig|1704024.3.peg.1660; -.
DR Proteomes; UP000052010; 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 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 2A-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}.
FT DOMAIN 75..223
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 274..361
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 377..473
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 516..568
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 581 AA; 63506 MW; 539780668F6C7872 CRC64;
MGFSEEVKIL SKKYISAGDH GSSDYFALIK ELVSWRNRHE KGSAEFAVWQ EEIDRIYGFI
GDELISNDAR PITPVKFGTS GWRGIIGKDL YVKSVQQVTQ AIVAVFQGIE GYPELAKALG
VETFSAAQTR GCVVGFDNRF GGGILAQAVI DVLTDSGIRV HYAGESTTGV LSAALLELDA
AFSVNLTPSH NPLEYGGYKF NGSDGGPAAS LITDLITQKA RQIIDEDPPI TVSKDRELVR
EFDSLESWVG MVRRNRKFHS LDYDAIISNF ASDPEVVLAV DCVHGASRLH IKKLINGGFS
GPSHDRLIIL RGETDPTFGG VAPEPSSANM KPVINALAVR PESLKLGAVI DPDGDRIRMT
DGTVEIDMNL FGGMAYHFLH EIKGLSGMVA KTVATSNFAN QLAEDFGEDV FESKVGFKEF
KPVIGKALVY FEESDGISVI GHTPEKDAYI GLLLGLDMVM TLRKNLGEYL LEIQKKHGFY
YPAKDGVIVS CQGKQLLTIL SGLEQYTPGS VIRVGDEDRK IAKVIDIDGR KMVLDDGSWL
MIRPSGTEPK VRFYVEAREK KKQIALFAAA KAMLDEIGLL N
//
