ID S3KG47_TREMA Unreviewed; 588 AA.
AC S3KG47;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9194_01550 {ECO:0000313|EMBL:EPF31207.1};
OS Treponema maltophilum ATCC 51939.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125699 {ECO:0000313|EMBL:EPF31207.1, ECO:0000313|Proteomes:UP000014541};
RN [1] {ECO:0000313|EMBL:EPF31207.1, ECO:0000313|Proteomes:UP000014541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51939 {ECO:0000313|EMBL:EPF31207.1,
RC ECO:0000313|Proteomes:UP000014541};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Blanton J.M.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Treponema maltophilum ATCC 51939.";
RL Submitted (APR-2013) 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:EPF31207.1}.
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DR EMBL; ATFF01000006; EPF31207.1; -; Genomic_DNA.
DR RefSeq; WP_016525818.1; NZ_KE332518.1.
DR AlphaFoldDB; S3KG47; -.
DR STRING; 1125699.HMPREF9194_01550; -.
DR PATRIC; fig|1125699.3.peg.1562; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_12; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000014541; 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; 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000014541}.
FT DOMAIN 47..188
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 214..317
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 330..456
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 588 AA; 65254 MW; 37D295E8874DA545 CRC64;
MDTNEIIARA KQYIAQETNE VFRSEVEKLV KDNDIKELEE RFYQSLEFGT GGLRGIIGGG
TNRMNTLMIH KATQGLANYC IKALPEQAAA GKLSAAIAYD SRKYSDVFAE ETACIFAANG
FTVYLFTSLR PTPELSFAIR TFGCTTGVVV TASHNPPQYN GYKAYWSDGA QVTPPHDTGI
IDEVNKVNSI KIISKDEGVR QGKIILIDND VDEKYWAMCK RQLFRPELIK QKAKDVRVVY
TPLHGTGAMH VEKVLGDLGL TVITVPEQRK PDGNFPTVEK PNPEEAPALK MAIELAKKEK
ADAVMATDPD ADRFGSAVPA ANGEWVLISG NQMGVLFTDY IIVSRKELNK MPKNPAIIRS
IVTSPMVDYI AKANGVHVDE CLTGFKWIAS VMNRYDTKRD YNYIFGFEES YGYNVETEVR
DKDGVSASAM CAEMTLYWRS QGKSLLERLE ELYKTYGYFE DRAISKNFLG ASGVQTMKAI
MSKLRKEGLK TLGGKKVVMI RDVGEGFSYD PENPHKKQKL DIPSSNVLQF FLEDGSIVSA
RPSGTEPKIK FYINAVVLDS PSLDAAKKDA DKLCSAIEKE IQAVLDAS
//
