ID A0A0P7H8E0_9EURY Unreviewed; 379 AA.
AC A0A0P7H8E0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KPN29765.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:KPN29765.1};
GN Name=glmM_1 {ECO:0000313|EMBL:KPN29765.1};
GN ORFNames=SY89_00482 {ECO:0000313|EMBL:KPN29765.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN29765.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|EMBL:KPN29765.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CDK2 {ECO:0000313|EMBL:KPN29765.1};
RA Kaushik R., Gaba S., Singh R.N., Abrol S., Yadav A.N., Saxena A.K.;
RT "Genome sequence of extreme halophilic archaea of Halolamina pelagica CDK2
RT isolated from Rann of Kutch, India.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPN29765.1}.
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DR EMBL; LGUC01000001; KPN29765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7H8E0; -.
DR STRING; 699431.SY89_00482; -.
DR PATRIC; fig|699431.3.peg.502; -.
DR Proteomes; UP000050535; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
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; 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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KPN29765.1};
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:UP000050535}.
FT DOMAIN 11..53
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 72..173
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 178..288
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 314..372
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 379 AA; 40317 MW; 2EE7C4E78526E700 CRC64;
MRYAEVEGVP AVVVTASHNP PEYNGIKLVG ADGVELPVAE LERVEDCLLG ETFEEAGWDA
TGNSRRIDGV ADDYVDDLLA NVDRAAIADA GLTVALDPGH GAGALTSPEF FRRLGCEVVT
VNGQPDGHFP GRNPEPVPEN LDDLGRLVRA ADADVGIAHD GDADRAIFFD EAGEYVEGDA
SLAALAAEAL EPGDATVAAV NVSQRLVDVC DEVGADLELT PIGATNIITR IQELQAGGRR
VPIAGEGNGG IFFPNYRLVR DGAFIAAKFL ELLATSGETP SEVVEPYTAY ENVRRNLAYD
EEAELSTMLS AAEQYAADAD VEAETVDGYR LDYGDAWVLV RPSGTEPKVR IYAEARERDR
AVELADAVED ELAAALDDD
//
