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Database: UniProt
Entry: A0A135VX82_9ARCH
LinkDB: A0A135VX82_9ARCH
Original site: A0A135VX82_9ARCH 
ID   A0A135VX82_9ARCH        Unreviewed;       458 AA.
AC   A0A135VX82;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Phosphoglucosamine mutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AM326_05635 {ECO:0000313|EMBL:KXH77149.1};
OS   Candidatus Thorarchaeota archaeon SMTZ-45.
OC   Archaea; Asgard group; Candidatus Thorarchaeota.
OX   NCBI_TaxID=1706443 {ECO:0000313|EMBL:KXH77149.1, ECO:0000313|Proteomes:UP000070599};
RN   [1] {ECO:0000313|EMBL:KXH77149.1, ECO:0000313|Proteomes:UP000070599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ-45 {ECO:0000313|EMBL:KXH77149.1};
RX   PubMed=26824177;
RA   Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT   "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT   phylum with pathways for acetogenesis and sulfur reduction.";
RL   ISME J. 0:0-0(2016).
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:KXH77149.1}.
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DR   EMBL; LRSM01000011; KXH77149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135VX82; -.
DR   Proteomes; UP000070599; 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          4..133
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          152..253
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          258..366
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          396..445
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   458 AA;  49825 MW;  A126122C85A302E0 CRC64;
     MTGKLFGTTG VRKVYSEEFD LEMALNLGKA LGTYVGSGSV VIARDARTTG LMIADTVTAG
     ILSTGVNVIR AGIIPTPTLA FITMKHGFDA GVMITASHNP PQYTGLKFWS RNSMGFTAKE
     ETKLEEIYNK KNFKVANWDE LGKESRFEDS VEEHIEALLK RCDADAIRSK TFRVIVDPGN
     GAACVLTPYL MQRLNCHVVT INGQLDGHFP GRRSEPDEES LGDLIQMIKQ TGADLGIAHD
     GDSDRVIFVT EQGEVIKGDR TIALLAQQAM LASKRGTVVT TVDSSLVLDE TVRRAGGNII
     RTPVGDIQVA IKVAESNGVI GGEACGVYIF PEAHLAPEPF LAVCRVLELM ARTEKTFGEL
     IATIPQYPII RSKLECPNDK KESVMKSISE TLPSKMRNVK EVLTVDGLGI TMEQGWILVR
     PSGTEPIIRI TCEGQTREAV EEILRTSEEV VRATIASA
//
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