ID B3CAY7_9BACE Unreviewed; 580 AA.
AC B3CAY7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II {ECO:0000313|EMBL:EDV04239.1};
GN ORFNames=BACINT_03372 {ECO:0000313|EMBL:EDV04239.1};
OS Bacteroides intestinalis DSM 17393.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV04239.1, ECO:0000313|Proteomes:UP000004596};
RN [1] {ECO:0000313|EMBL:EDV04239.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV04239.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDV04239.1, ECO:0000313|Proteomes:UP000004596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV04239.1,
RC ECO:0000313|Proteomes:UP000004596};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2008) 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:EDV04239.1}.
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DR EMBL; ABJL02000008; EDV04239.1; -; Genomic_DNA.
DR RefSeq; WP_007664783.1; NZ_ABJL02000008.1.
DR AlphaFoldDB; B3CAY7; -.
DR STRING; 471870.BACINT_03372; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000004596; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05799; PGM2; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
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 51..188
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 213..318
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 519..551
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 580 AA; 64417 MW; 315514391D482A43 CRC64;
MENQELIKQV TEKAQRWLTP AYDAETQAEV KRMLENEDKT ELIDCFYKDL EFGTGGLRGI
MGAGTNRMNI YTVGAATQGL SNYLNKCFKD KEQISVVVGY DCRNNSDKFA QISADIFSAN
GIKVYLFDDL RPTPEVSFAI RHFGCQSGIN ITASHNPREY NGYKAYWDDG AQVLAPHDTA
IIDEVNKVTV ADIKFKGNKD LIQTIGADVD KIYLDMVHSI SIDPEVIKRQ KDLSIVYTPL
HGAGRVLIPA SLKEWGFENV NCVPEQMVKD GNFPTVVSPN PENAEALSMA IALAKKIDAD
IVMASDPDAD RVGMACKDDK GEWVLINGNQ TCLIFLYYII KNRIAMGKMQ PNDFIVKTIV
TTELIKAVAD KNKIEMRDCY TGFKWIAREI RLSEGKQQYI GGGEESYGFL AEDFVRDKDA
VSACSLLAEI CAWAKDQGKT LYDVLMDIYV EYGFSKETTV NVVKPGKSGA DEIKAIMDNF
RANPPKEIGG SPVKLIKDYK TLKITDAEGK VSELDMPEAS NVLQYFTEDG TKISVRPSGT
EPKIKFYIEV KGEMGCPKCY ASADAEAEEK VVAVRKSLGI
//
