ID A0A0R2R0I4_9FLAO Unreviewed; 378 AA.
AC A0A0R2R0I4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KRO54635.1};
DE Flags: Fragment;
GN ORFNames=ABR79_02215 {ECO:0000313|EMBL:KRO54635.1};
OS Cryomorphaceae bacterium BACL11 MAG-121001-bin54.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655587 {ECO:0000313|EMBL:KRO54635.1, ECO:0000313|Proteomes:UP000051874};
RN [1] {ECO:0000313|EMBL:KRO54635.1, ECO:0000313|Proteomes:UP000051874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL11 MAG-121001-bin54 {ECO:0000313|EMBL:KRO54635.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRO54635.1}.
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; LIBL01000183; KRO54635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2R0I4; -.
DR Proteomes; UP000051874; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326}.
FT DOMAIN 4..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 163..259
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 263..373
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT NON_TER 378
FT /evidence="ECO:0000313|EMBL:KRO54635.1"
SQ SEQUENCE 378 AA; 41450 MW; B01A9E0285150185 CRC64;
MTKIKFGTDG WRAIIAQEYT TDNVARVSIA VAHWLNEKYK NPSVVIGHDC RFAGELFAET
TAKVLASKGI LVKLAKGFVS TPMVSLGVVK EKANLGIVIT ASHNPPSYNG YKLKGDFGGP
LLQADITDVE RRIPEINSVD YTAILIEDLV AKGKVVYVDL EDIYCKHAEA YFDLDAIRNS
TMNFAYDAMY GAGMNAVKRL LPNATLLHCE NNPGFLGTAP EPIHRNLQEF SDLMKNNALD
CGLATDGDAD RIGLYDSKGN FIDSHHIILL LIHYLVKYKG MKGKVVTAFS CSVKVEQMCN
YYGLDQETVQ IGFKHIAGKM VTEDVLLGGE ESGGIATAGH IPERDGIWIG LILFEFMAKS
GKSLEDLIAE VYEIVGPF
//
