ID A0A0K2GD12_NITMO Unreviewed; 547 AA.
AC A0A0K2GD12;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ALA58477.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ALA58477.1};
GN Name=pgm {ECO:0000313|EMBL:ALA58477.1};
GN ORFNames=NITMOv2_2060 {ECO:0000313|EMBL:ALA58477.1};
OS Nitrospira moscoviensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA58477.1, ECO:0000313|Proteomes:UP000069205};
RN [1] {ECO:0000313|EMBL:ALA58477.1, ECO:0000313|Proteomes:UP000069205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA58477.1,
RC ECO:0000313|Proteomes:UP000069205};
RX PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA Nielsen P.H., Wagner M., Daims H.;
RT "Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria
RT from the genus Nitrospira.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(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 ---------------------------------------------------------------------------
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; CP011801; ALA58477.1; -; Genomic_DNA.
DR RefSeq; WP_053379640.1; NZ_CP011801.1.
DR AlphaFoldDB; A0A0K2GD12; -.
DR STRING; 42253.NITMOv2_2060; -.
DR KEGG; nmv:NITMOv2_2060; -.
DR PATRIC; fig|42253.5.peg.2032; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000069205; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 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, ECO:0000313|EMBL:ALA58477.1};
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:UP000069205}.
FT DOMAIN 39..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..439
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 491..536
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 547 AA; 59165 MW; A0943C623ADD1D44 CRC64;
MSLHPLAGKP APVSMLVDVP HLLAAYTEQP DVNVPQQRVS FGTSGHRGSS LKRSFNERHV
LAVTQAVCEY RAAQKTTGPL FLGMDTHALS RPAFETALEV LAANRVEVRI DRDGGFTPTP
VISHAILTYN RGRTAGLADG IVITPSHNPP EDGGIKYNPP EGGPADTDVT KWIESRANAL
LAAQLHGVAR MPYEQARRTS TVHGHDYVGA YVGDLAQVID LDAIKQARLQ LGVDPLGGSG
VAYWKPIADR YGLNIEIVNP SVDPTFRFMP LDWDGKIRMD CSSPYAMANL IALKDRFDVA
FGNDADNDRH GIVTKSGGLM NPNHYLAAAI FYLFSHRPGW TVGAGIGKTL VSSSLIDRVA
AKLTRRLVEV PVGFKWFVPG LLEGSLGFGG EESAGASFLR RDGTVWTTDK DGIIMDLLAA
EMMAKTGRDL SEWYRQLTED LGEPVYERID AAAMPEQKAI LANLSPDQVK ATHLAGDPIT
AMLTTAPGNG AAIGGLKVVT EHGWFAARPS GTEDVYKLYA ESFRGKEHLK RIQVEAQSLI
GRVLSGK
//
