ID V4XWY6_9ARCH Unreviewed; 459 AA.
AC V4XWY6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ESS03087.1};
GN ORFNames=A07HR67_02597 {ECO:0000313|EMBL:ESS03087.1};
OS uncultured archaeon A07HR67.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412871 {ECO:0000313|EMBL:ESS03087.1, ECO:0000313|Proteomes:UP000030660};
RN [1] {ECO:0000313|Proteomes:UP000030660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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; KI543168; ESS03087.1; -; Genomic_DNA.
DR AlphaFoldDB; V4XWY6; -.
DR STRING; 1412871.A07HR67_02597; -.
DR PATRIC; fig|1412871.3.peg.2744; -.
DR Proteomes; UP000030660; Unassembled WGS sequence.
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; cd05800; PGM_like2; 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; 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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030660}.
FT DOMAIN 5..134
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 158..251
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 262..354
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 377..454
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 459 AA; 48833 MW; 37D1817591F22EE0 CRC64;
MDEISFGTDG WRATLDTFTD DRVRIVGQAV ADHLDAAGHD EPVAVGYDAR ETSEGFAESL
AEVLSGNGFD VLLPERDVPT PVIAYGIVDN DLAGACMVTA SHNPPEYNGV KFIPNDGAPA
LPDVTEDIVS RLAEPDLLPE AERGEVRRHD FVSAHAEAAR ELVDADLDGL TVAYDAMHGS
GRGVTDALLA SAGAEVRRLR CDRDPTFGGA SPEPSAEHLE ALAATVTDPD TDVDLGIAND
GDSDRVAVVT PERGVLDANL FYAACYDRLL ETDAGPAVRT VSTTFLVDRI AEAHGQAVFE
TPVGFKWVAE AMAEHDALFG GEESGGFSVR GHVREKDGVL MALLAADATD AEPFDERVDR
LLAEHGQIAA GKVSIECPDD RKAAVLDELD DHIPDSVAGH PVAEVVTLDG FKLLLENGSW
LLVRPSGTEP KLRVYAESDA DDRVETLLAA GRELVEPLV
//
