ID Q2LST5_SYNAS Unreviewed; 562 AA.
AC Q2LST5;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ABC77141.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ABC77141.1};
GN ORFNames=SYN_01343 {ECO:0000313|EMBL:ABC77141.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77141.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77141.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77141.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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}.
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DR EMBL; CP000252; ABC77141.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LST5; -.
DR STRING; 56780.SYN_01343; -.
DR KEGG; sat:SYN_01343; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_016950_8_1_7; -.
DR InParanoid; Q2LST5; -.
DR Proteomes; UP000001933; Chromosome.
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 CDD; cd05801; PGM_like3; 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; 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:ABC77141.1};
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:UP000001933}.
FT DOMAIN 52..192
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 223..327
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 334..454
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 501..552
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 562 AA; 61239 MW; 24B9A05E1BBAF7AF CRC64;
MKFIHLFFRR RLMLLHPLAG KPVPPTLLAN IPRLVSSYYT LHPDAAREAQ RVAFGTSGHR
GTPENGTFNE DHVLAVCQAI CDYRKEMSLS GPLFLGMDTH ALSEPAWATA LEVLAANGVM
VFIQEGRGYT PTPVISHAIL TWNEGHFPDH ADGIVITPSH NPPEDGGIKY NPPHGGPADT
TVTADIEKRT NAYLAAGLWG VRRMPLKQAL DGDCVKPYDY IQPYVDDLQN VIDMEAVAGA
VLKIGADPMG GSGLAFWDRI AGRYGLNIEV VNPHADPTFS FMTLDRDGKI RMDCSSPYAM
ARLIDLKDRF DIAFGNDPDF DRHGIVTRSA GLMNPNAYLA VAIDYLFRNR PQWGPEVAIG
KTLVSSGMID RIAASLERRL CEVPVGFKWF VSGLLAGQLG FGGEESAGAS FLRRDGRAWT
TDKDGIIMDL LAAEIIARTG RDPGELFASL TERFGDSLYD RMDVAATPEQ KAVLKKLSPA
QVSASELAGE RILATLTEAP GNGAPIDGLK VVTENGWFAA RPSGTENIYK IYLESFKGKE
HLERIREEAQ ALVSATFTAA GV
//
