ID H0ACJ5_HALSG Unreviewed; 425 AA.
AC H0ACJ5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EHK01497.1};
GN ORFNames=HRED_02446 {ECO:0000313|EMBL:EHK01497.1};
OS Haloredivivus sp. (strain G17).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Candidatus Haloredivivus.
OX NCBI_TaxID=1072681 {ECO:0000313|EMBL:EHK01497.1, ECO:0000313|Proteomes:UP000003484};
RN [1] {ECO:0000313|EMBL:EHK01497.1, ECO:0000313|Proteomes:UP000003484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G17 {ECO:0000313|EMBL:EHK01497.1,
RC ECO:0000313|Proteomes:UP000003484};
RA Ghai R., Pasic L., Fernandez A.B., Martin-Cuadrado A.-B., Mizuno C.M.,
RA McMahon K.D., Papke R.T., Stepanauskas R., Rodriguez-Brito B., Rohwer F.,
RA Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "New Dominant Microbial Groups Along A Salinity Gradient.";
RL Sci. Rep. 0:0-0(2011).
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:EHK01497.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGNT01000190; EHK01497.1; -; Genomic_DNA.
DR AlphaFoldDB; H0ACJ5; -.
DR Proteomes; UP000003484; 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 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 PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003484}.
FT DOMAIN 5..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 151..245
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 255..332
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 353..415
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 425 AA; 47681 MW; C051C97F5656DB0F CRC64;
MRPEKVFKRY DIRGKYSEEL DEEFSERLGK ALGTFIIQNY KHQAVVGRDN KESSKGLKKS
LIEGLISTGV DVIDVGEGPT DFAAWSGMKK DCVSVEVTSS HMPLEFNGFK LMYPKGNGFV
NEDLYAVQNI FREKEFVSGS GSISERPDLK DEYMDEIADF ASQFSEEDER KIVVDSLGGT
AKILPELLRR LGHEVIDISE KTRPYTDPPN PKPEKLEKLK ERVEDEDAYL GISNDLDADR
VTAYHNERFL SGDEVFCILS QLVEGSVVAS IDTTQGLKDL KEVEYTRVGD PFVMDKALEI
DAELAGEPNG HYSFTDFVPS NSGILTALIL SGLDLEEKLS KIPDYEVRRT SIPVEDKHKV
IEALKENFSG DIISELDGVK FRYQDAEVLV RPSGSSPKVR VIAEAENKKE ANKALNKTLD
RINQF
//
