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Database: UniProt
Entry: X0SG02_9ZZZZ
LinkDB: X0SG02_9ZZZZ
Original site: X0SG02_9ZZZZ 
ID   X0SG02_9ZZZZ            Unreviewed;       475 AA.
AC   X0SG02;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Phosphoglucosamine mutase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=S01H1_01412 {ECO:0000313|EMBL:GAF79934.1};
OS   marine sediment metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=412755 {ECO:0000313|EMBL:GAF79934.1};
RN   [1] {ECO:0000313|EMBL:GAF79934.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAF79934.1};
RX   PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA   Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA   Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA   Takami H.;
RT   "High frequency of phylogenetically diverse reductive dehalogenase-
RT   homologous genes in deep subseafloor sedimentary metagenomes.";
RL   Front. Microbiol. 5:80-80(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}.
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:GAF79934.1}.
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DR   EMBL; BARS01000609; GAF79934.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0SG02; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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.
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}.
FT   DOMAIN          12..148
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          168..266
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          273..385
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          404..456
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAF79934.1"
FT   NON_TER         475
FT                   /evidence="ECO:0000313|EMBL:GAF79934.1"
SQ   SEQUENCE   475 AA;  52789 MW;  CBFAB756658683E1 CRC64;
     IIKAKIKKMT SNIFGTSGIR MVFQNYSETD LMFTPQMALD VGLALGTYLK GDGIVVIGKD
     IRTSALPIEY ALISGILSTG CNVKTLGIVT TPTLALSQRF LDAKAGVMIT ASHNTPEYIG
     LKFWNPSGIG YSHEQEEEIS RIYDEKDFLD IKWDQIGRVT QVNDINDKHI SEIRNLIEFD
     GSNLNVIVDP GNGAGCEIVP KLLSAYKVNI ITINAQMDGT FPGRNSEPSE KNLIQISKFL
     KISTQKDIGI ALDGDADRVI FLDETGEIVD PIRLLALLAK YYIQNNKNNL SMNDMKVSTP
     VNSSSLIDDV LQPLGCEVLR TEVGDIQVAQ ALRENGGFLG GETSGTYIWP SFHLGPDSIV
     TIGIVLQMMV KTGKTLIDLL KEVPKYPYYR KQFQLIKDIP FTDEINQKIV TEMKESFDSM
     GKKIKTINKM DGCRFDYDDG WILIRRSGTS PYLRISGESN IDINQSIEMN KIAED
//
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