ID A0A087A980_9BIFI Unreviewed; 558 AA.
AC A0A087A980;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Alpha-D-glucose phosphate-specificphosphoglucomutase {ECO:0000313|EMBL:KFI55330.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KFI55330.1};
GN ORFNames=BCAL_1347 {ECO:0000313|EMBL:KFI55330.1};
OS Bifidobacterium callitrichos DSM 23973.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437609 {ECO:0000313|EMBL:KFI55330.1, ECO:0000313|Proteomes:UP000029072};
RN [1] {ECO:0000313|EMBL:KFI55330.1, ECO:0000313|Proteomes:UP000029072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23973 {ECO:0000313|EMBL:KFI55330.1,
RC ECO:0000313|Proteomes:UP000029072};
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:KFI55330.1}.
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DR EMBL; JGYS01000006; KFI55330.1; -; Genomic_DNA.
DR RefSeq; WP_043164453.1; NZ_JGYS01000006.1.
DR AlphaFoldDB; A0A087A980; -.
DR STRING; 1437609.BCAL_1347; -.
DR eggNOG; COG0033; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000029072; 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:KFI55330.1};
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 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; 60377 MW; A66BA10A80A69A05 CRC64;
MVANNAGKPA TPADLINVDE VIGKYYDLVP DPAVPEQRVI FGTSGHRGSS LKTSFNEAHI
VAISQAIAEY RKKAGVTGPL YLGSDTHALS EPARKTAIEV LVANGVHVRV DSRGDFVPTP
VVSQAILTHN RAADGTQRFE GEGLADGIVV TPSHNPPTDG GFKYDPVTGG PAPAETTNAI
AARANELLAD YKNVKRVPYE EAIKSEYVEP FDFREHYVAD LGNVIDFDVI RSSGVRLGID
PLGGASVNYW PLINEKYNLN IGVVRPEVDP TWRFMTIDHD GKIRMDPSSP YAMKGLVDEL
NAGAWDKYDL VGGTDPDADR HGIVCPDWGV MNPNHYIAVC VEYLFGGNRP GWPEGAAVGK
TLVSSSLIDR VAASINAKVM EVPVGFKWFV DPLFKGEVAF GGEESSGMSF LRKDGRIWTT
DKDGLIPDLL AAEITAKTGK NPAELHKDQV ARFGESWYKR VDTPTTLEQK QKFGKLTGDD
VTATQLAGED ITAKLTEAPG NHAKIGGLKV TTKDNWFAAR PSGTENIYKV YAESFESPEA
LDKVLAEAEV VVDKALAE
//
