ID A0A109BDK1_HYPSL Unreviewed; 501 AA.
AC A0A109BDK1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KWT66801.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:KWT66801.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:KWT66801.1};
GN ORFNames=APY04_2208 {ECO:0000313|EMBL:KWT66801.1};
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT66801.1, ECO:0000313|Proteomes:UP000059074};
RN [1] {ECO:0000313|EMBL:KWT66801.1, ECO:0000313|Proteomes:UP000059074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT66801.1,
RC ECO:0000313|Proteomes:UP000059074};
RA Albers P.;
RT "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT consortium.";
RL Submitted (OCT-2015) 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}.
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:KWT66801.1}.
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DR EMBL; LMTR01000071; KWT66801.1; -; Genomic_DNA.
DR RefSeq; WP_068462425.1; NZ_LMTR01000071.1.
DR AlphaFoldDB; A0A109BDK1; -.
DR STRING; 121290.APY04_2208; -.
DR PATRIC; fig|121290.4.peg.2410; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000059074; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
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:KWT66801.1};
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:UP000059074}.
FT DOMAIN 26..157
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 175..272
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..392
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 410..486
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 501 AA; 54633 MW; F3760B8F9DD3D445 CRC64;
MLPKPRADLK PNTADFERIP LVKPTGFREY DARWLFPQEI NLLGLTAVGL GMATLFEERG
VPKRIVTGHD YRSYSASVKQ ALINGLLAGG CEVHDIGLAL SPMAYFAQFD LDVEGVAMVT
ASHNDNGWTG IKMGLNRPLT FGPDEMSRLK EIVLSGTSKP AGGGRLIFVP DMAERYMRAL
ADRPKLKRKL KVVAACGNGT AGAFAPQVLE AVGCEVVPLD TQLDYTFPRY NPNPEDMGML
HAIAEAVVQH KADVGFGFDG DGDRCGVVDN EGNEIFADTV GVMLARDISA QHKDAVFVAD
VKSTGLFMTD PVLIENGAKT LYWKTGHSYM KRYTFEQKAL VGFEKSGHFF FQPPLGRGYD
DGLVAALAVC DMLQRAPDKT MADLRRALPK TYQSPTMSPH CDDEKKYGVV DRVVAHYQKL
AADGGTVAGQ KIRDLVTVNG VRVTLEDGTW GLVRASSNKP ELVVVVESPV SEANMKAIFA
DIDGLLSQQP EVGEYNQKIE V
//
