ID   K2I5Z2_BIFBI            Unreviewed;       558 AA.
AC   K2I5Z2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:BBA47542.1};
GN   ORFNames=BBJK_00749 {ECO:0000313|EMBL:BBA47542.1};
OS   Bifidobacterium bifidum LMG 13195.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1207542 {ECO:0000313|EMBL:BBA47542.1, ECO:0000313|Proteomes:UP000262177};
RN   [1] {ECO:0000313|EMBL:BBA47542.1, ECO:0000313|Proteomes:UP000262177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7004 {ECO:0000313|EMBL:BBA47542.1,
RC   ECO:0000313|Proteomes:UP000262177};
RX   PubMed=28814130; DOI=10.1080/09168451.2017.1361810;
RA   Katoh T., Maeshibu T., Kikkawa K., Gotoh A., Tomabechi Y., Nakamura M.,
RA   Liao W.-H., Yamaguchi M., Ashida H., Yamamoto K., Katayama T.;
RT   "Identification and characterization of a sulfoglycosidase from
RT   Bifidobacterium bifidum implicated in mucin glycan utilization.";
RL   Biosci. Biotechnol. Biochem. 81:2018-2027(2017).
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}.
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DR   EMBL; AP018131; BBA47542.1; -; Genomic_DNA.
DR   RefSeq; WP_003814621.1; NZ_JSEA01000004.1.
DR   GeneID; 56627928; -.
DR   Proteomes; UP000262177; Chromosome.
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};
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..452
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          497..549
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   558 AA;  60187 MW;  FF0AEC5B6081039A CRC64;
     MVANNAGKPA TPADLINVDE VIGKYYDLVP DPAVPEQRVI FGTSGHRGSS LKTSFNEAHI
     VAITQAIAEY RKKAGVTGPL YLGRDTHALS GPAEKTAIEV LVANGVHVRV DSRGDFVPTP
     VVSQAILTHN RAADGTQRFE GEGLADGIVV TPSHNPPTDG GFKYDPVTGG PAPAETTNAI
     AARANELLGD FKSIKRVPYE EAIKSEYVEG FDFREHYVAD LGNVIDFDVI RDSGVRLGID
     PLGGASVNYW PLINEKYGLN IGVVRPEVDP TWRFMTIDHD GKIRMDPSSP YAMKGLVDQL
     NAGAWDKYDL VGGTDPDADR HGIVCPNWGV MNPNHYIAVC VEYLFGGNRP GWPEGTGIGK
     TLVSSSLIDR VASSINAKLV EVPVGFKWFV DPLFSGEVAF GGEESSGMSF LRRDGRVWTT
     DKDGLIPDLL AAEITAKTGK NPAQLHQDQV ARFGESWYKR VDTPTTLEQK AKFAKLTGDD
     VAATQLAGED ITAKLTEAPG NHAKIGGLKV TTKDNWFAAR PSGTENIYKV YAESFVSPEA
     LDKVLDEAKL VVDKALGE
//