ID U1NFU3_9EURY Unreviewed; 468 AA.
AC U1NFU3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ERH02245.1};
GN ORFNames=J07HN6_01813 {ECO:0000313|EMBL:ERH02245.1};
OS Halonotius sp. J07HN6.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halonotius.
OX NCBI_TaxID=1238427 {ECO:0000313|EMBL:ERH02245.1, ECO:0000313|Proteomes:UP000030638};
RN [1] {ECO:0000313|EMBL:ERH02245.1, ECO:0000313|Proteomes:UP000030638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HN6 {ECO:0000313|Proteomes:UP000030638};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; KE356568; ERH02245.1; -; Genomic_DNA.
DR AlphaFoldDB; U1NFU3; -.
DR HOGENOM; CLU_016950_7_1_2; -.
DR Proteomes; UP000030638; 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; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
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; 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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030638}.
FT DOMAIN 2..131
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 171..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 401..459
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 468 AA; 48607 MW; 1BFAB3745E0E91FC CRC64;
MIEFGTAGIR GPVEETVTPR VALRVGSAVG RFAVAHGSAS TPAVVIGRDG RTTGSGLVAA
VEAGVSAAGS RPIRVGQLPT PALGFASRGR FGVMLTASHN PPADNGIKCF ADGRAFDDEQ
EAWIEQAVDN EAVAGFDEWG TTHRETPLTD YRAAVVDYTR ERAGGDSPCA GLDIAVDCGN
GMAALATPRV LRDLGANVTA LNANVDGHFP GRPSKPTPET LGDLQAFVAD GDADLGIAHD
GDADRIVVLD GDGEIIHEDT AVAILAGYYT RRGSSVDGDT TDDPVVVTTP NASARIDEAV
AAAGGRVERV RLGALHEGIA AAEADGGRVV FAAEPWKHLH SAFGGWIDGV VSAAVISSLA
ASEGLAALRE PITERPYRKV SIDCPERAKT PAMTALETSL PAAFDDVTLS LDHGVRLDRS
DGSWLLVRPS GTEPYIRLYA ESEAVDEIVA TATERIEAAV DDATETAD
//
