ID Q2LTT8_SYNAS Unreviewed; 409 AA.
AC Q2LTT8;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABC77496.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:ABC77496.1};
GN ORFNames=SYN_00891 {ECO:0000313|EMBL:ABC77496.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77496.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77496.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77496.1,
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 -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000256|ARBA:ARBA00002315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000256|ARBA:ARBA00000370};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|ARBA:ARBA00004921}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. A-PGAM subfamily. {ECO:0000256|ARBA:ARBA00005524}.
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DR EMBL; CP000252; ABC77496.1; -; Genomic_DNA.
DR RefSeq; WP_011417518.1; NC_007759.1.
DR AlphaFoldDB; Q2LTT8; -.
DR STRING; 56780.SYN_00891; -.
DR KEGG; sat:SYN_00891; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_2_0_7; -.
DR InParanoid; Q2LTT8; -.
DR OrthoDB; 9804453at2; -.
DR Proteomes; UP000001933; Chromosome.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd16011; iPGM_like; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 2.
DR Gene3D; 3.30.70.2130; Metalloenzyme domain; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR023665; ApgAM_prokaryotes.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR NCBIfam; TIGR00306; apgM; 1.
DR NCBIfam; TIGR02535; hyp_Hser_kinase; 1.
DR PANTHER; PTHR31209:SF4; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR Pfam; PF10143; PhosphMutase; 1.
DR PIRSF; PIRSF006392; IPGAM_arch; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABC77496.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT DOMAIN 1..376
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 409 AA; 44920 MW; D342D3DBDFD24D4E CRC64;
MKYVIILGDG MADYPIDEID GKTPLEAACT PNMDQMAAEG TLGLIDTIPH GLQPGSDVAN
LSVLGYDPLE TYTGRGPLEA ASLGLELESG DVAFRCNLVT LGPIENPMME DFTSGHISSG
EAQEIINDLN KEMGSDTYRF YPGVGYRHLM VWRRGQEALE TTPPHDITGR SVYHYLPRGE
GADQVIRLMK RSQKILKDHP VNRNRISAGL KPANSIWLWG QGKAPKIVRL TDRYSIRGGM
ISAVDLLNGI GKYAGLEKIH VEGVTGYTDT NYAGKAEQAL AALKDMDFVF IHVEAPDEMG
HEGSLAGKIR SIEDLDKKVV GTVLEGIKNF NDYRVLVLSD HPTPIILRTH SGEPSPFAVL
SSEKHENMAS GWSFCESSAK KSGLFISPGH HLMDLFLKGW RSFIEEKHS
//
