ID M6DC67_9LEPT Unreviewed; 609 AA.
AC M6DC67;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Putative phosphoglucomutase {ECO:0000313|EMBL:EMJ96155.1};
GN ORFNames=LEP1GSC194_0516 {ECO:0000313|EMBL:EMJ96155.1};
OS Leptospira alstonii serovar Sichuan str. 79601.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218565 {ECO:0000313|EMBL:EMJ96155.1, ECO:0000313|Proteomes:UP000011988};
RN [1] {ECO:0000313|EMBL:EMJ96155.1, ECO:0000313|Proteomes:UP000011988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=79601 {ECO:0000313|EMBL:EMJ96155.1,
RC ECO:0000313|Proteomes:UP000011988};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Galloway R.L., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-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}.
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:EMJ96155.1}.
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DR EMBL; ANIK01000028; EMJ96155.1; -; Genomic_DNA.
DR AlphaFoldDB; M6DC67; -.
DR PATRIC; fig|1218565.3.peg.1506; -.
DR Proteomes; UP000011988; 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;
FT DOMAIN 70..205
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 251..341
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 351..470
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 609 AA; 67253 MW; 736BD24156D740B3 CRC64;
MNLKRKPIFM NLILLKKLNR NPMNHPESFI HSWTRDPFPS GVRDEAKRAL EKFSNGESGP
DVEAFSVPLE FGTGGMRGKL GNGIGRMNEF TVGRAALGFV SYLSKKNKKA SIVIAYDSRR
RSKEFAEVTA GIAASLGVKV ILFSEVTPTP LLSYAIRYYK ASGGVVITAS HNPPDYNGFK
AYLSDGGQLV PPDDQKIISK IESITDWNRI IILSPKDPLY KKMVKPAGKD CFVSYKKELA
KAGILSTSLK SKDRAAMKIV YSPLHGTGAK TMKELLNGFG YKNVFLVPEQ KDPDGEFPTV
KYPNPEEPEA MELSKKFAIA KGADAFIATD PDADRLGIGV KNGNGDYVLL NGNQIGSIMA
AYLCEAYAAS KKKKKAVLIK TIVTTDLQEI IAKRNHVKYK NVLTGFKFIA QVMAKIDKSK
TDFFLFGGEE SFGYLPVSFV RDKDSLSSAL LLLEILTEKK DLLHYMDEIY LKYGLFQESL
KSLTLEGSAG KEKIRKSLES LRTVDLLGKQ IHRRKIIGIL DYKTRTVKGS ASKTAFAGCP
SSDVIQVILE GNAKLTIRPS GTEPKIKIYS SFQSLKTPTS KEEIRNLTED LLSEIKASEE
IFLTLAGLS
//
