ID Q3SVR3_NITWN Unreviewed; 499 AA.
AC Q3SVR3;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:ABA03628.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:ABA03628.1};
GN OrderedLocusNames=Nwi_0361 {ECO:0000313|EMBL:ABA03628.1};
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA03628.1, ECO:0000313|Proteomes:UP000002531};
RN [1] {ECO:0000313|EMBL:ABA03628.1, ECO:0000313|Proteomes:UP000002531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC {ECO:0000313|Proteomes:UP000002531};
RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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}.
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DR EMBL; CP000115; ABA03628.1; -; Genomic_DNA.
DR RefSeq; WP_011313693.1; NC_007406.1.
DR AlphaFoldDB; Q3SVR3; -.
DR STRING; 323098.Nwi_0361; -.
DR KEGG; nwi:Nwi_0361; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_5; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000002531; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; 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, ECO:0000313|EMBL:ABA03628.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002531}.
FT DOMAIN 26..154
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 176..272
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..390
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 423..486
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 499 AA; 54458 MW; 78D418A75B1A55FE CRC64;
MFPKPKSVLA PNTYAYESEP MVKATGFREY DARWLFGKEI NLMGIQALGM GLGTLIGELG
QKKEIVTGHD FRSYSSSIKY ALISGLLASG CKVHDIGLCM TPMAYFAQFE LDVPCVAMVT
ASHNDNGWTG VKMGANRPLT FGPDEMTRLK EIVLGAAFAG RGGGSYEFHD NFPSRYIADL
TKRPKLKRRL KAVVACGNGT AGAFAPQVME AIGCEVIPLD TELDHSFPKY NPNPEDMKML
HAIRDAVLEN KADLGLGFDG DGDRCGVVDN TGEEIFADKV GVMLARDMSA IHKDAHFVVD
VKSTGLFVTD PVLQQQGARA TYWKTGHSYM KRRTHELGAL AGFEKSGHFF FNAPMGRGYD
DGLISAIAVC EMLDRAAGKS LADLKNALPK TWSSPTMSPH CADEAKYGIV DSVVKHFEDA
RANGDKVAGQ PIRDLVTVNG IRVTAQDGSW GLVRASSNKP ELVVVVESPV SEQRMRDMFE
AMDSVLRTHP EVGEYNQKI
//
