ID M0MT02_HALMO Unreviewed; 460 AA.
AC M0MT02;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain I {ECO:0000313|EMBL:EMA48751.1};
GN ORFNames=C448_02743 {ECO:0000313|EMBL:EMA48751.1};
OS Halococcus morrhuae DSM 1307.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=931277 {ECO:0000313|EMBL:EMA48751.1, ECO:0000313|Proteomes:UP000011568};
RN [1] {ECO:0000313|EMBL:EMA48751.1, ECO:0000313|Proteomes:UP000011568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1307 {ECO:0000313|EMBL:EMA48751.1,
RC ECO:0000313|Proteomes:UP000011568};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:EMA48751.1}.
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DR EMBL; AOMC01000046; EMA48751.1; -; Genomic_DNA.
DR RefSeq; WP_004051741.1; NZ_AOMC01000046.1.
DR AlphaFoldDB; M0MT02; -.
DR STRING; 931277.C448_02743; -.
DR PATRIC; fig|931277.6.peg.532; -.
DR eggNOG; arCOG00767; Archaea.
DR OrthoDB; 10363at2157; -.
DR Proteomes; UP000011568; 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; 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; IPR016066; A-D-PHexomutase_CS.
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; 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:UP000011568}.
FT DOMAIN 5..132
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 165..252
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 262..362
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 376..452
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 460 AA; 48854 MW; B5133D52560F260B CRC64;
MDAISFGTDG WRATLDVFTA PRVRMVGQAV ATHLDGRDAP VGVCYDARES SRGFAEELAR
VLAANGFDVL LPERDRPTPL LAWAIDDRDL AGGLMVTASH NPADYNGVKF IPDDGAPALP
EVTESIEANL AEPEPLPEAE WGTIQETGFV ASHAEHAHDL VAEYADEAAL DDLTVAYDAM
HGSGRGVTDE LLSEAGASVE RLRCERAPDF GGTPPEPSAE HLTELATRVQ NGDASLGIAN
DGDADRLAVV TPERGHLDEN LFFAALYDFL LESASGPAVR TVSTTFLIDR IAEAHGESVV
ETAVGFKWVA RAMAEAGALV GGEESGGFSV DGHVREKDGV LLALLAAAAE REESLDDRVD
RLLDEHGEIH QSKISVDCPD DEKARVLDEL EGGLPDRVAG EPVADIVTKD GFKTVLESGA
WLLVRPSGTE PVLRVYAEAE SGERVAALLD AGEELVAPLV
//
