ID A0A151BHZ7_9ARCH Unreviewed; 454 AA.
AC A0A151BHZ7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KYH39362.1};
GN ORFNames=AYL28_000330 {ECO:0000313|EMBL:KYH39362.1};
OS Candidatus Bathyarchaeota archaeon B23.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779367 {ECO:0000313|EMBL:KYH39362.1, ECO:0000313|Proteomes:UP000075353};
RN [1] {ECO:0000313|EMBL:KYH39362.1, ECO:0000313|Proteomes:UP000075353}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B23 {ECO:0000313|EMBL:KYH39362.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (MAR-2016) 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:KYH39362.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LUCA01000002; KYH39362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BHZ7; -.
DR PATRIC; fig|1779367.3.peg.25; -.
DR Proteomes; UP000075353; 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..130
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 152..247
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 252..360
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 368..440
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 454 AA; 48400 MW; 526749DDCDEBEE7F CRC64;
MRGLFGTSGI RGVVNVELTP QLALEVGKAI ATLHRGGVLV VGRDTRPSGE MLEASLIAGA
ASCGCDVEAL GLAPTPLTAY TTRALSADTG VSVTASHNPP EYNGLKPFDS SGMAYGEERR
RAVEEVIRSE AYTPSEWSGI GLVEEIEATP LYLDAILRDL ELQRAWRVAC DLMNGATAVT
APEALKAAGC EGVYLNANPD GYFPSGVPEP RGETLRRLGE VVRSSEAQVG FAFDGDGDRV
MFVDEDGVAP TPDRVLAAYA AYVVERCRGG VIVTHVGASM CVDEAVRLAG GRVIRTRVGD
AYVAEALMRR GGVFGGEPVG AWIHPDVHPC PDGLLSALRL LGALEERDVS LSEFVAEIPE
YPLLRGKVRC PNPLKGRVMA LLRERWGEHL GGVLSTSTVD GLRLELGDGW LLMRPSGTEP
VIRLTAEAES RSRAEELMER GRGLVEEAVR RSGG
//