ID M2XXW1_9NOCA Unreviewed; 491 AA.
AC M2XXW1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:EME65826.1};
GN ORFNames=G352_08092 {ECO:0000313|EMBL:EME65826.1};
OS Rhodococcus ruber BKS 20-38.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1278076 {ECO:0000313|EMBL:EME65826.1, ECO:0000313|Proteomes:UP000011731};
RN [1] {ECO:0000313|EMBL:EME65826.1, ECO:0000313|Proteomes:UP000011731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BKS 20-38 {ECO:0000313|EMBL:EME65826.1,
RC ECO:0000313|Proteomes:UP000011731};
RX PubMed=23558535;
RA Bala M., Kumar S., Raghava G.P., Mayilraj S.;
RT "Draft Genome Sequence of Rhodococcus ruber Strain BKS 20-38.";
RL Genome Announc. 1:E0013913-E0013913(2013).
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:EME65826.1}.
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DR EMBL; AOEX01000027; EME65826.1; -; Genomic_DNA.
DR RefSeq; WP_003935715.1; NZ_AOEX01000027.1.
DR AlphaFoldDB; M2XXW1; -.
DR PATRIC; fig|1278076.4.peg.1685; -.
DR Proteomes; UP000011731; 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; 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 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 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};
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 4..138
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 161..257
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 270..375
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 429..467
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 491 AA; 50493 MW; F3F010C077799F11 CRC64;
MSLRFGTAGL RGPVGDGPGC INEDVVVRTT AGLARWLRAR GSGGGTVVVG RDARTGSAEF
FTAATEVLAA AGFAVVALPR PLPTPVTAYA VRTLDAVAGV QITASHNPAS DNGYKVYTRG
GAQLVEPDDR EIEKAIDAVG AASSVPRTAV APAGDDLVAR YLTRVASLPR ATARTLRIAL
TPLHGVGGET AVAALHAAGF DDVHVVDAQF APDPRFPTVE FPNPEEPGAA DAVLALAADV
GADIALALDP DADRCAVGVP TPAGWRMLRG DETGALLGDR ILAGAPRGAL VATTIVSSTL
LGKLAAARGA RYAQTLTGFK WLARAGDGLV YAYEEALGHC VDPDAVRDKD GIATAVVVAD
YAAELKARRS TLVDALDALY REFGLHLGDQ VSIRVTDLAR IGAIMSRLRS ALPAELAGEP
VTATDLATAS GPLRTDAVVL EGASVRVVVR PSGTEPKLKC YLEAVATDGD RDGASARLQA
LRAWATGLGE P
//
