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Database: UniProt
Entry: V4YBT4_9ARCH
LinkDB: V4YBT4_9ARCH
Original site: V4YBT4_9ARCH 
ID   V4YBT4_9ARCH            Unreviewed;       445 AA.
AC   V4YBT4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:ESS08567.1};
GN   ORFNames=A07HN63_01798 {ECO:0000313|EMBL:ESS08567.1};
OS   uncultured archaeon A07HN63.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=1412873 {ECO:0000313|EMBL:ESS08567.1, ECO:0000313|Proteomes:UP000030667};
RN   [1] {ECO:0000313|Proteomes:UP000030667}
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, ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; KI543217; ESS08567.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4YBT4; -.
DR   STRING; 1412873.A07HN63_01798; -.
DR   PATRIC; fig|1412873.3.peg.1906; -.
DR   Proteomes; UP000030667; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03087; PGM_like1; 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; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR024086; GlmM_arc-type.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
DR   PANTHER; PTHR42946:SF6; PHOSPHOGLUCOSAMINE MUTASE; 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.
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}.
FT   DOMAIN          2..127
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          154..248
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          254..355
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          369..440
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   445 AA;  46187 MW;  275B1D5087E4FC9A CRC64;
     MFGTSGIRGP VGDAVTADLA LDVGRAVATD GAETVVIGRD ARDSGRFLLD AAAAGCRECG
     ADVIDLGLAA TPTLARSIAR LDADAGIVIT ASHNPPEDNG LKLWTPSGQA FDTDRRERIT
     EIIESEAYEY APWDESGTRR TDDHGDTAHS TAIRDAISDD AVATMDGLTA VVDVGNGVGS
     VTARTLTTLG VSVTTLNAQP DGAFPGRPSE PTAETLNTLC AQVGGTDADF GIAHDGDADR
     MVAVDEAGRF VPKDVLLALF ARRAVVDADG GVVAAPVDTS QCVDDAIEPV GGRVTRTKVG
     DVFVAEAATR DEVVFGGEPS GAWIWPEETL CPDGSLAAVK LAVMVATEGS LAAQVDGVAT
     YPIRRDSVEV DDKDGVMERV ADGLLADYDD VTTIDGVRVE TDAGWVLIRP SGTQPLIRVT
     AEADTDDAAD RLAADAVERI EAARE
//
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