ID U2MET2_TRESO Unreviewed; 594 AA.
AC U2MET2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I {ECO:0000313|EMBL:ERF60637.1};
GN ORFNames=HMPREF1325_0297 {ECO:0000313|EMBL:ERF60637.1};
OS Treponema socranskii subsp. socranskii VPI DR56BR1116 = ATCC 35536.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=1125725 {ECO:0000313|EMBL:ERF60637.1, ECO:0000313|Proteomes:UP000016412};
RN [1] {ECO:0000313|EMBL:ERF60637.1, ECO:0000313|Proteomes:UP000016412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VPI DR56BR1116 {ECO:0000313|EMBL:ERF60637.1,
RC ECO:0000313|Proteomes:UP000016412};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-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:ERF60637.1}.
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DR EMBL; AUZJ01000037; ERF60637.1; -; Genomic_DNA.
DR RefSeq; WP_021330420.1; NZ_AVQI01000068.1.
DR AlphaFoldDB; U2MET2; -.
DR STRING; 1125725.HMPREF1325_0297; -.
DR PATRIC; fig|1125725.3.peg.1402; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000016412; 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}.
FT DOMAIN 47..189
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 220..323
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 329..456
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 594 AA; 65498 MW; D99B8FD6A64053A2 CRC64;
MEKSEILKRA NAYIAEEKDE NFRSEVESLI AKDDIKELED RFYQSLEFGT GGLRGIMGGG
TNRMNPLVIN RATQGLASYV IKAFPEKAKA GTLSAVLAYD SRKNSDVFAE AAACIFAANG
IKAYLFSSLR PTPELSFAVR TLGADTGVIV TASHNPRIYN GYKVYWNDGA QVIPPHDKGI
IGEVNAVKEI KTMSKDKAIK AGKIVLIDKD MDEKFWDMCK AQLFRPDLIK AHAKDVKIVY
TPLHGTGGMH VEKVLGDLGL NVITVPEQRD PDGNFPTVEK PNPEEAPAMK LAIALGEKEK
ADCIMATDPD ADRFGSAFPD KDGKFVLITG NQMGALFLEY ILLSRKEFGK MPEKPAAVRT
IVTSPFIDYI CKKYGVKVFE CLTGFKWIAA VEAEMEKDKS ASYVFGFEES YGYKIEKEVF
DKDGISASAM CAEMTLYWRS KGKSLLEHLD DMYKEYGYFE DKTIEQYFPG PTGGEAMRGI
MTKLRNEGLK TLGGKRVKEI RDIERSVSFD PANPATTKPL DLPKSNVLQF FLDDGTIVSA
RPSGTEPKIK FYINCTVPVA GNNDAGLAQA KKEAAHLRDA IASEIKSTLD AAAE
//