ID W2VKU5_9BIFI Unreviewed; 577 AA.
AC W2VKU5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:ETO98257.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ETO98257.1};
GN Name=pgm {ECO:0000313|EMBL:ETO98257.1};
GN ORFNames=HMPREF1494_0205 {ECO:0000313|EMBL:ETO98257.1};
OS Bifidobacterium sp. MSTE12.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1161409 {ECO:0000313|EMBL:ETO98257.1, ECO:0000313|Proteomes:UP000018909};
RN [1] {ECO:0000313|EMBL:ETO98257.1, ECO:0000313|Proteomes:UP000018909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSTE12 {ECO:0000313|EMBL:ETO98257.1,
RC ECO:0000313|Proteomes:UP000018909};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (DEC-2013) 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:ETO98257.1}.
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; AZYA01000007; ETO98257.1; -; Genomic_DNA.
DR AlphaFoldDB; W2VKU5; -.
DR PATRIC; fig|1161409.3.peg.299; -.
DR Proteomes; UP000018909; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 Pfam; PF00408; PGM_PMM_IV; 1.
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, ECO:0000313|EMBL:ETO98257.1};
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 58..205
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 235..344
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 351..472
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 516..571
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 577 AA; 62910 MW; 03FD76CB95CFA3BA CRC64;
MNTIWRLRAH RPKAWQNGAM VANNAGMPAT PEDLINVDEV IGKYYDVVPD PSVPEQRVSF
GTSGHRGSSL KTSFNEAHIV AITQAIAEYR KKAGVTGPLY IGRDTHALSE PAWKTAIEVL
VANGVTVRID SRDDFTPTPV VSQAILTHNR AADGTQRFTG EGLADGIVVT PSHNPPTDGG
FKYDPVTGGP APSDVTNAIA DRANELLGDF RNVKRVPFDQ AVKSDLVERF DYRDHYVSDL
ENVIDFDVIR SSGVRLGIDP LGGASVNYWP LMNEKFNLTI DVVRPQVDPT WSFMTIDHDG
KIRMDPSSPY AMKGLVDSLN NGAWDKYDLV GGTDPDADRH GIVCPNWGVM NPNHYIAVCV
EYLFGGNRPG WPEGAGIGKT LVSSSLIDRV AASINAKLVE VPVGFKWFVD PLFKGEVAFG
GEESSGMSFL RKDGRVWTTD KDGLIPDLLA AEITAKTGKN PAQLHQEQVE RFGESWYKRV
DTPTTLEQKI KFGKLSGDDV EATQLAGEDI TAKLTEAPGN HAKIGGLKVT TKNNWFAARP
SGTENIYKVY AESFESPEAL DKVLAEATEV VDKALAD
//
