ID R5ZF72_9ACTN Unreviewed; 466 AA.
AC R5ZF72;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase alpha/beta/alpha domain II {ECO:0000313|EMBL:CDA35234.1};
GN ORFNames=BN511_00536 {ECO:0000313|EMBL:CDA35234.1};
OS Collinsella sp. CAG:166.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=1262850 {ECO:0000313|EMBL:CDA35234.1, ECO:0000313|Proteomes:UP000018358};
RN [1] {ECO:0000313|EMBL:CDA35234.1, ECO:0000313|Proteomes:UP000018358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:166 {ECO:0000313|Proteomes:UP000018358};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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:CDA35234.1}.
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DR EMBL; CBBR010000047; CDA35234.1; -; Genomic_DNA.
DR AlphaFoldDB; R5ZF72; -.
DR Proteomes; UP000018358; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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; 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; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 6..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..254
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 259..366
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 418..454
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 466 AA; 50087 MW; 730C5C7CD9E2A620 CRC64;
MCAIIHFGTD GWRARVDEDF TADNVARIAD AVGELWQKTN PGKTVYIGFD TRPLASEFAE
LAAGVLAAHG LDAVLASRPV PTPALTWAAA YDGEACGALM VTGSHHPQGY LCLKIRMGDG
STANQDVIEE LEETMAPEPM EIEGQYRTAD IIPDYMQAVA SFVDAEAIRA AHLRVVVDPM
GGAAQGYLAD LLRELGVEVH EIHAGQASDQ EDICPDPVEP WVDACERTVI EDGACAGLVT
DGDADRIGAV DERGRYIHPH QIMALVLGDL VQFRNLEGRV VVNLSCSTLV RRIAEALGCR
VTVKPVGFKY IAAEMKKGGV LIGGEEAGGI GIAAHMPERD GILACLILCE LMAKTDAPLG
VLVDQLEDSF GKTSYGRRDL RLEAEDAETL RTLLPGVNPK SICGKVPQNV SHMDGLRLAF
EDDTWLLVRP SGTEPVVRVY AEGFSVEERD ELLDAGCALA RGTYPL
//
