ID I7CMA0_NATSJ Unreviewed; 445 AA.
AC I7CMA0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:AFO58944.1};
GN OrderedLocusNames=NJ7G_3728 {ECO:0000313|EMBL:AFO58944.1};
OS Natrinema sp. (strain J7-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO58944.1, ECO:0000313|Proteomes:UP000006507};
RN [1] {ECO:0000313|EMBL:AFO58944.1, ECO:0000313|Proteomes:UP000006507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J7-2 {ECO:0000313|EMBL:AFO58944.1,
RC ECO:0000313|Proteomes:UP000006507};
RX PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA Shen P., Wang L., Tang B., Tang X.F.;
RT "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT of growth on synthetic media without amino acid supplements.";
RL PLoS ONE 7:E41621-E41621(2012).
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; CP003412; AFO58944.1; -; Genomic_DNA.
DR RefSeq; WP_014865416.1; NC_018224.1.
DR AlphaFoldDB; I7CMA0; -.
DR STRING; 406552.NJ7G_3728; -.
DR GeneID; 13351565; -.
DR KEGG; nat:NJ7G_3728; -.
DR PATRIC; fig|406552.5.peg.3272; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_7_1_2; -.
DR OrthoDB; 10363at2157; -.
DR Proteomes; UP000006507; 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 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; 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 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 6..127
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 151..243
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 249..353
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 388..433
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 445 AA; 45762 MW; 6C1C156FD594E21E CRC64;
MVGPRGIGGP GGEEITAARA LSVGRAVASD GSDRVVVGRN ARATGAVLAD AVTAGLRECG
ADVLAVGVAP TPTIARTVSR TDATAGIVVT AAHDSTSDDG LMLRTASGKA VSPEQRAAIA
ARVERGEYDL HPRDGRGSTE TVADASERHV TELVEAVSVA DPPSVVVDVG DGAGEITARV
LSALGCDVGT LHGRREEAVP GWPGEPVGEA FGALSSLVEA TDARLGIAHD GDADRMLAVD
ETGAVVPRDV LLALFARATA TDGDIVVVPV GTSMAVDDAL ATVGVTVRRT QVGDTFVADC
TTWPDVAFGG DPSGAWIWPD ETPSPDGPLA ACKLVELVAD RGPLSSLAAA IETYPSRRAS
VAVEEQTAVM NQVRECAHEW YDDVDTLGGV YVDVGAGWLF LRASDTEPVI HLTVEARDEF
RAERLEADAI GLLETAIATV SGLRP
//
