ID A0A1D8IJT7_9GAMM Unreviewed; 459 AA.
AC A0A1D8IJT7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=BI364_00580 {ECO:0000313|EMBL:AOU96713.1};
OS Acidihalobacter yilgarnensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Acidihalobacter.
OX NCBI_TaxID=2819280 {ECO:0000313|EMBL:AOU96713.1, ECO:0000313|Proteomes:UP000095401};
RN [1] {ECO:0000313|Proteomes:UP000095401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F5 {ECO:0000313|Proteomes:UP000095401};
RA Khaleque H.N., Ramsay J.P., Kaksonen A.H., Boxall N.J., Watkin E.L.J.;
RT "Acidihalobacter prosperus F5.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC EC=5.4.2.8; Evidence={ECO:0000256|ARBA:ARBA00000586};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 2/2. {ECO:0000256|ARBA:ARBA00004699}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; CP017415; AOU96713.1; -; Genomic_DNA.
DR RefSeq; WP_070077107.1; NZ_CP017415.1.
DR AlphaFoldDB; A0A1D8IJT7; -.
DR KEGG; aprs:BI364_00580; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000095401; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 8..138
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 153..250
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 256..363
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 370..444
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 459 AA; 49847 MW; 20A5BC9F661581D1 CRC64;
MTAIASSLFR AYDIRGVVDD TLTEDAVHHI GRAFGSEALA QGQHAVVIGR DGRLSGPTLI
AVLADGLRST GIDVIDVGAV PTPVVYFAAE DLGTRTCIAL TGSHNPPQYN GLKLVIDGRT
LHSEGIQTLR ERIERDDYAR GQGSLRSLDI GQRYLDRITS DVHLARPLKV GVDCGNGVAG
ELAPRLIEAL GCTVTPLFCE IDGRFPNHHP NPSEPENLAD LIACVRTQGL DLGLAFDGDG
DRLGVVDGEG RVVWADRQMI LYAADVLARN PSATIIFDIK CSRHLAEAIR AHGGEALMWK
TGHSLIKAKM QETGALLAGE MSGHVFFKER WYGFDDGLYT AARLLEILSQ DARTPTAVFA
ELPDSINTPE LNVHFAEEGA HFAFMQHLKA QADFGDARLT LIDGLRADYP DGWGLVRPSN
TTPSLVIRFE AEDVAGLERI QGIFRRQMLA VEPTLTLPF
//
