ID A0A0P9FUF8_9ARCH Unreviewed; 458 AA.
AC A0A0P9FUF8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative phosphoglucosamine mutase {ECO:0000313|EMBL:KPV62322.1};
GN Name=glmM_1 {ECO:0000313|EMBL:KPV62322.1};
GN ORFNames=AOA65_1946 {ECO:0000313|EMBL:KPV62322.1};
OS Candidatus Bathyarchaeota archaeon BA1.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV62322.1, ECO:0000313|Proteomes:UP000050312};
RN [1] {ECO:0000313|EMBL:KPV62322.1, ECO:0000313|Proteomes:UP000050312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA1 {ECO:0000313|EMBL:KPV62322.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
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:KPV62322.1}.
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DR EMBL; LIHJ01000081; KPV62322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9FUF8; -.
DR STRING; 1700835.AOA65_1946; -.
DR KEGG; barc:AOA65_1946; -.
DR Proteomes; UP000050312; 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: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};
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 154..254
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..366
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 391..443
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 458 AA; 50782 MW; 8D1A315EB51C4C65 CRC64;
MIRRKLFGTN GIRGVVNDDL TPEFVIRVGC AIGTFFECGK IVVGHDCRTS GLMLTQAVIV
GLTSTGCTVY DVGMAPTPAI QYAVKRHGMD GGVIITASHN PPEYNGIKVV AEDGVELPRE
REIEIESLFF NGKVRRVDWD KIGAIHRLPS ILDVYIEAIK QHVDVNAIQR RHFHVVVDPG
NGVGGLAAPY LLREMGCRVT TINANIDGTF PSRPPEPRPE NLRELASALR IVKADVGVAY
DGDADRSIFV DEKGEIHWGD RTFALIEKFF LQSNPGEIIV TPVSSSHLIK EIADQYGGRV
VWTKVGSIIV SHVMKKLNAK LGGEENGGIF YAPHQPVRDG AMATALILDV MAKTGKKLSE
LLAELPLYYI EKDRLECPDD LKERALKEFI EKTKDMTIDT IDGAKIWFPD TSSILIRPSG
TEPIYRFYAE GKTRNRAAQL IYEYKAKLHE IIDKSKDD
//
