ID Q0AE26_NITEC Unreviewed; 523 AA.
AC Q0AE26;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:ABI60406.1};
GN OrderedLocusNames=Neut_2184 {ECO:0000313|EMBL:ABI60406.1};
OS Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=335283 {ECO:0000313|EMBL:ABI60406.1, ECO:0000313|Proteomes:UP000001966};
RN [1] {ECO:0000313|EMBL:ABI60406.1, ECO:0000313|Proteomes:UP000001966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101675 / C91 / Nm57 {ECO:0000313|Proteomes:UP000001966};
RX PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT eutropha C91: implications for niche adaptation.";
RL Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI60406.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0AE26; -.
DR STRING; 335283.Neut_2184; -.
DR KEGG; net:Neut_2184; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_4; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000001966; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
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 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};
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 23..165
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 192..299
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 302..422
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 471..516
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 523 AA; 56735 MW; 567F77DE1D517F29 CRC64;
MITTWLNAFY SIQPDTSNPA QRVSFGTSGH RGSSLAGSFN ELHILAIAQA VVDYCQQADI
SGPLFLGLDT HALSRPAWDV VLQVLVANQI AVFVATERGV TATPLVSRAI LAHNAQHPTD
LADGLIITPS HNPPEDGGIK YNTPDGGPAD SDVTDWIEAR ANQYLQKQCA EVKRMDLQDA
LSQVQEYNYV AHYVAELGQV VDLPAIRQSG LKLGVDPMGG TGLPVWQALA LDPAFNITVV
NTSQAADFAF MPPDHDGRIR MDCSSPAAMA NLLKIRQQFD LSLANDPDAD RHGIVDAAGL
MNPNHFLCVC VDYLLTYRPL WSKSLKIGKT LVTSSLMDRI VAAHDRELYE VPVGFKWFVK
GLHQSWLAFA GEESAGASLL TFDGQTWTTD KDGIALCLLA AEISAVTGLT PSQYYAKLTE
QYGRPYYRRI DAPATAEQKA VFKTLTVAHI TATELAGEPI ELVLLNAPGN GASIGGIKVC
TENGWFAARP SGTEALYKIY AESFISEQHL QQLIDEGQTL LNL
//
