ID M6VYN1_LEPBO Unreviewed; 460 AA.
AC M6VYN1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:EMO62607.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:EMO62607.1};
GN Name=glmM {ECO:0000313|EMBL:EMO62607.1};
GN ORFNames=LEP1GSC133_1825 {ECO:0000313|EMBL:EMO62607.1};
OS Leptospira borgpetersenii serovar Pomona str. 200901868.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1192866 {ECO:0000313|EMBL:EMO62607.1, ECO:0000313|Proteomes:UP000012159};
RN [1] {ECO:0000313|EMBL:EMO62607.1, ECO:0000313|Proteomes:UP000012159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200901868 {ECO:0000313|EMBL:EMO62607.1,
RC ECO:0000313|Proteomes:UP000012159};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., 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, 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:EMO62607.1}.
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DR EMBL; AKWF02000076; EMO62607.1; -; Genomic_DNA.
DR AlphaFoldDB; M6VYN1; -.
DR STRING; 1192866.LEP1GSC133_1825; -.
DR Proteomes; UP000012159; 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:EMO62607.1};
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..141
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 280..376
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 404..452
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 460 AA; 49649 MW; 2F494A0E50CBB413 CRC64;
MNTKVPVFNH PDLMVSVSGI RGIIPTGLSP EVIFNALRAF GTWIEGSKVV IGRDSRPSGP
YIENIALGLM QAMGKDVLQL GIVPTPTVKA VVNLSKAGGG IMISASHNPI LWNAFKFIGP
GGFFTGAADL EQILDTIRNQ SYRQIQYKPS SKIVSGKEWS EKHIESVLKR VNVSAIRKKK
YKVLVDAVNG AGSALIPELL GKLGCKPILL HCSPDGTFPR PPEPTPDALK QTSRKMKSSG
ADIGFALDPD ADRLVVLTPK KGAISEEYTL PLSFLSLTLG KMPKKANLVV NLSTSFINEF
VAGQYSVPVS RSKVGEANVV SEMLRQKSIF GGEGNGGVID PAIASFGRDS LSGIAHILNG
MAATGKKIDS IVEELPAVHM QKTSFKVAGK NLQDIYSKFS EEFSAFSEET LDGLRLASED
SWIHIRPSNT EPIIRVIAEA RTKKDLNSLL DRSRSLMENA
//
