ID A0A0B0EHH6_9BACT Unreviewed; 425 AA.
AC A0A0B0EHH6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KHE90563.1};
DE Flags: Fragment;
GN ORFNames=SCABRO_03670 {ECO:0000313|EMBL:KHE90563.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE90563.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE90563.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE90563.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) 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}.
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:KHE90563.1}.
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; JRYO01000255; KHE90563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0EHH6; -.
DR PATRIC; fig|237368.3.peg.3955; -.
DR eggNOG; COG1109; Bacteria.
DR Proteomes; UP000030652; 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 15..64
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 98..195
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 200..321
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KHE90563.1"
SQ SEQUENCE 425 AA; 46332 MW; 20EF13B5FC2F1C62 CRC64;
YLIYKKIGNA SRGKIPSPAV ALYGIVNRVP AIMVTGSHIP SDRNGIKFNK PSGEILKADE
DGIRMQSVSV DDSLFAEAAG FVSPVTGKWD VSNVARDMYI ARYLDVFPND CLKGLRVAVY
QHSAVGRDII LDIVRGLGAD AEALGRSDTF IPVDTEAIRP EDVELAAKWA EKGVYDAIIS
TDGDSDRPLI ADERGRWLRG DVAGILCAKY LGADSVSTPV SCNSAVEKSG YFKKVCRTRI
GSPFVIESMN SESEGESDVI VVVGYEANGG FLINSNIPLF GKRLRALPTR DAVILHLSII
LLAVSEGKTV SEIVAGLPRR YTASDRLENF SQEQSRTILD KLNTGDVTKD KAVVTDIFGK
LCGNCCCLDR TDGVRMTFDS EEVIHLRPSG NAPEFRVYNE AATEDRVEEL NTACLKVLIK
MKEKN
//
