ID A0A0M2LKN7_9MICO Unreviewed; 550 AA.
AC A0A0M2LKN7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KKI16289.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:KKI16289.1};
GN ORFNames=XM48_15815 {ECO:0000313|EMBL:KKI16289.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI16289.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI16289.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI16289.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKI16289.1}.
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DR EMBL; LAYO01000111; KKI16289.1; -; Genomic_DNA.
DR RefSeq; WP_046456809.1; NZ_LAYO01000111.1.
DR AlphaFoldDB; A0A0M2LKN7; -.
DR STRING; 1642040.XM48_15815; -.
DR PATRIC; fig|1642040.3.peg.962; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
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 Pfam; PF00408; PGM_PMM_IV; 1.
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:KKI16289.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033836}.
FT DOMAIN 38..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 214..319
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..443
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 494..544
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 550 AA; 58558 MW; A08BF9FF75C6C606 CRC64;
MHDRAAAPAR PEDLVDLEAL LAAFDERVPD PSDPAQRVVF GTSGHRGSSL DGSFNAAHII
AMSAAIAEYR AEQGIAGPLF LGADTHPLSA PAERIAREVL SAAGVRVLAR SGTGDEIYVP
TPAVSHAILT HNRGRDAADP DRADGIVVTP SHNPPRDGGF KYNPPHGGPA DTDATGWIAR
RANELLERGV DAIPRAGRDS VAGEPVGRYD FLGEYVESLD RVIDLDAIRR SGLRIGAHPL
GGASVAYWAA IRDRYELDLT VLGPGVDPRW SFMHLDWDGK IRMDPSSAQV MSTVTGYRDD
FDLVTGNDAD ADRHGIVTAD AGLMNPNHFL VVAIDYLLSH RPDWAPEAGI GKTLVSSGLI
DRVVAAHRRT LLEVPVGFKW FVPGLVDGSV VFGGEESAGA SFLRFDGAPW STDKDGILLC
LLAAEIQAVT GQSPSQRYRE LADRLGDPAY ARVDAPATPE QKARLAALAP SDVTDTELAG
DPITAVLTTA PGNGAGIGGL KVQTEHAWFA ARPSGTEHVM KIYAESFRGP EHLAQVQEAA
RRLVDRVLGA
//
