ID J9A7Z3_ENTFC Unreviewed; 500 AA.
AC J9A7Z3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II {ECO:0000313|EMBL:EJV58410.1};
GN ORFNames=HMPREF1345_00043 {ECO:0000313|EMBL:EJV58410.1};
OS Enterococcus faecium TX1337RF.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1134802 {ECO:0000313|EMBL:EJV58410.1, ECO:0000313|Proteomes:UP000003117};
RN [1] {ECO:0000313|EMBL:EJV58410.1, ECO:0000313|Proteomes:UP000003117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX1337RF {ECO:0000313|EMBL:EJV58410.1,
RC ECO:0000313|Proteomes:UP000003117};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-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:EJV58410.1}.
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DR EMBL; AMAA01000001; EJV58410.1; -; Genomic_DNA.
DR RefSeq; WP_002347729.1; NZ_JH804698.1.
DR AlphaFoldDB; J9A7Z3; -.
DR PATRIC; fig|1134802.3.peg.40; -.
DR HOGENOM; CLU_016950_6_0_9; -.
DR Proteomes; UP000003117; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
FT DOMAIN 8..143
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 167..273
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..392
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 500 AA; 55680 MW; 0A921B982F292FE1 CRC64;
MQDMKALQNE SDIRGIALPV EGHEVNLTTD RVEKIGWGLA NWLKKKKKST NPTKKWTIGI
GHDSRISGPA LKEALIQSLK EQGIHVIDFE LATTPAMFMS TQFEQFSCDA AVMLTASHLP
YYYNGIKFFT SEGGAEKEDI AYILSQQQKI NSEQVGSVEK ADLLIPYAQD LVTKIKKGMG
TQDDKPLKGW KIIVDAGNGA GGFFAEKVLN SLGADTTGSQ FLEPDGRFPN HIPNPDNKEA
MESIKQAVLA NEADLGIIFD TDVDRSAVVS ASGTVINRNN LIAVLSTIVL KEHPETRIVT
NSPTSSHLQK FIEEKGGTQI RYISGYRNVI NKALELNRLG KDTQLAIETS GHAAFKENYF
LDDGAYVIAK ILMLLPELKR KGITLDEQIK ELKQPVEVQE IRLKLFSDEP REQGNKILEE
MKRLLEEEKG MNFDPANEEG IRYNLQEPYG SGWFLIRLSL HEPLLVLQIE NDESGKNQLV
LEKLANLFGH FSDLGSLPAE
//
