ID A0A087DR46_9BIFI Unreviewed; 561 AA.
AC A0A087DR46;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KFI97996.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KFI97996.1};
GN ORFNames=BSTEL_0756 {ECO:0000313|EMBL:KFI97996.1};
OS Bifidobacterium stellenboschense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=762211 {ECO:0000313|EMBL:KFI97996.1, ECO:0000313|Proteomes:UP000029004};
RN [1] {ECO:0000313|EMBL:KFI97996.1, ECO:0000313|Proteomes:UP000029004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23968 {ECO:0000313|EMBL:KFI97996.1,
RC ECO:0000313|Proteomes:UP000029004};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI97996.1}.
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DR EMBL; JGZP01000010; KFI97996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087DR46; -.
DR STRING; 762211.BSTEL_0756; -.
DR eggNOG; COG0033; Bacteria.
DR Proteomes; UP000029004; 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:KFI97996.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000029004}.
FT DOMAIN 42..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 219..328
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 335..456
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 500..555
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 561 AA; 60473 MW; 935F0B886733EC33 CRC64;
MGFMVANNAG KPATPEDLIN VDEVIGKYYD LVPDPSVPEQ RVIFGTSGHR GSSLKTSFNE
AHIVAISQAI AEYRKKAGVT GPLYLGSDTH ALSGPAKKTA IEVLVANGVH VRIDSRDDFV
PTPVVSQAIL THNRAADGTQ RFEGEGLADG IVVTPSHNPP TDGGFKYDPV TGGPAPADVT
NAIAARANEL LGDYKNVKRV PYEEAVKSEY VEGFDFREHY VADLGNVIDF DVIRNSGVRL
GIDPLGGASV NYWPLINEKY GLNIGVVRPE VDPTWRFMTI DHDGKIRMDP SSPYAMKGLV
DQLNAGAWDK YDLVGGTDPD ADRHGIVCPD WGVMNPNHYI AVCVEYLFGG NRPGWPKGAA
VGKTLVSSSL IDRVAASIGA KVLEVPVGFK WFVDPLFSGE VAFGGEESSG MSFLRRDGRV
WTTDKDGLIP DLLAAEITAK TGKNPAELHK DQVARFGESW YKRVDTPTTL EQKQKFASLS
GDDVTATQLA GEDITAKLTE APGNHAKIGG LKVTTKDNWF AARPSGTENI YKVYAESFES
PEALDKVLAE ASEVVDKALG E
//
