ID M3FNX7_LEPIR Unreviewed; 460 AA.
AC M3FNX7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:EMG09144.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:EMG09144.1};
GN Name=glmM {ECO:0000313|EMBL:EMG09144.1};
GN ORFNames=LEP1GSC151_4870 {ECO:0000313|EMBL:EMG09144.1};
OS Leptospira interrogans serovar Grippotyphosa str. LT2186.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1001599 {ECO:0000313|EMBL:EMG09144.1, ECO:0000313|Proteomes:UP000011776};
RN [1] {ECO:0000313|EMBL:EMG09144.1, ECO:0000313|Proteomes:UP000011776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2186 {ECO:0000313|EMBL:EMG09144.1,
RC ECO:0000313|Proteomes:UP000011776};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Tulsiani S.M., Graham G.C., Burns M.-A.,
RA Dohnt M.F., Smythe L.D., McKay D.B., Craig S.B., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (FEB-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:EMG09144.1}.
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DR EMBL; AFME02000340; EMG09144.1; -; Genomic_DNA.
DR AlphaFoldDB; M3FNX7; -.
DR Proteomes; UP000011776; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05803; PGM_like4; 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; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
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 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; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EMG09144.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 17..140
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 162..260
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 282..377
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 391..452
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 460 AA; 50251 MW; 3F5368736C18B71F CRC64;
MNTKIPVFNH PDLMVSVSGI RGIIPTGLSP EVIFNSLRAF GTWIEGSKIV IGRDSRPSGS
YLENIALGLM QAMGKEVLQL GIVPTPTVKA VVNLSKAGGG IMISASHNPI IWNAFKFIGP
GGFFTNASDL EQILETVQNQ SYKPIQYKPS SKIVFGTEWS EKHIESVLKR VDVNSIRKKK
YKVLIDSING AGSYLVPELL KKLGCKPILL HCVPDGTFPR PPEPTPEALK QTSRKMKSSG
ADIGFALDPD ADRLVVLTPK KGAISEEYTL PLSFLSLTLE KIPKKANIVV NLSTSFINEF
VARQNGVPVF RSKVGEANVV SEMLRQKSIF GGEGNGGVID PTIASFGRDS LSGIAHILNV
MAATGKKIDS IVEELPAIYM QKTSFKIAGK NLQDIYSKFR GEFSTFSEET IDGLRLTSED
SWIHIRPSNT EPIIRIIGEA RTKKDLNSLL DRAGRLMENA
//
