ID B7GN89_BIFLS Unreviewed; 558 AA.
AC B7GN89; E8MN34;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Phosphoglucomutase, alpha-D-glucose phosphate-specific {ECO:0000313|EMBL:ACJ53245.1};
GN OrderedLocusNames=Blon_2184 {ECO:0000313|EMBL:ACJ53245.1};
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=391904 {ECO:0000313|EMBL:ACJ53245.1, ECO:0000313|Proteomes:UP000001360};
RN [1] {ECO:0000313|EMBL:ACJ53245.1, ECO:0000313|Proteomes:UP000001360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI]
RC {ECO:0000313|Proteomes:UP000001360};
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
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 ---------------------------------------------------------------------------
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; CP001095; ACJ53245.1; -; Genomic_DNA.
DR RefSeq; WP_012578445.1; NZ_JDTT01000049.1.
DR AlphaFoldDB; B7GN89; -.
DR KEGG; bln:Blon_2184; -.
DR PATRIC; fig|391904.8.peg.2261; -.
DR Proteomes; UP000001360; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
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};
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 39..186
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 216..325
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 332..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 497..547
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 558 AA; 60224 MW; 998A78F04E9BCD01 CRC64;
MVANNAGQPA TPADLINVDE VIGKYYDLVP DPEVPEQRVI FGTSGHRGSS LKTSFNEAHI
IAISQAIAEY RKKAGVTGPL YLGSDTHALS GPAKKTAIEV LVANGVHVRV DSRDDFVPTP
VVSQAILTHN RAADGTPRFE GEGLADGIVV TPSHNPPTDG GFKYDPVTGG PAPAETTNAI
AARANELLGD FKSIKRVPYE EAIKSEYVEG FDFREHYVDD LENVIDFDVI RNSGVRLGID
PLGGASVNYW PLINEKYGLN IGVVRPEVDP TWRFMTIDHD GKIRMDPSSP YAMKGLVDEL
NAGAWDKYDL VGGTDPDADR HGIVCPNWGV MNPNHYIAVC VEYLFGGNRP GWPEGAAVGK
TLVSSSLIDR VAASIDAKVI EVPVGFKWFV DPLFSGEVAF GGEESSGMSF LRKDGRVWTT
DKDGLIPDLL AAEITAKTGK NPAQLHQEQV ERFGESWYKR VDTPTTLEQK AKFAALSGDD
VTASTLAGED ITAKLTEAPG NHAKIGGLKV TTKDNWFAAR PSGTENIYKV YAESFVSPEA
LDKVLDEATV VVDKALSE
//
