ID Q2LPI3_SYNAS Unreviewed; 433 AA.
AC Q2LPI3;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABC76012.1};
GN ORFNames=SYN_00621 {ECO:0000313|EMBL:ABC76012.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC76012.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC76012.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC76012.1,
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; ABC76012.1; -; Genomic_DNA.
DR RefSeq; WP_011416047.1; NC_007759.1.
DR AlphaFoldDB; Q2LPI3; -.
DR STRING; 56780.SYN_00621; -.
DR KEGG; sat:SYN_00621; -.
DR eggNOG; COG3635; Bacteria.
DR HOGENOM; CLU_034906_1_0_7; -.
DR InParanoid; Q2LPI3; -.
DR OrthoDB; 9804453at2; -.
DR Proteomes; UP000001933; Chromosome.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:InterPro.
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; IPR006124; Metalloenzyme.
DR InterPro; IPR004456; Pglycerate_mutase_ApgM.
DR InterPro; IPR042253; Pglycerate_mutase_ApgM_sf.
DR NCBIfam; TIGR00306; apgM; 1.
DR PANTHER; PTHR31209; COFACTOR-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR31209:SF0; METALLOENZYME DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT DOMAIN 1..403
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 433 AA; 47674 MW; EAA5EFB1C1761035 CRC64;
MRCILLLLDG LGDRSHPVLD GQTPLQAADT PNLDKIAAIG MNGLFHSHLQ GAALPSELAH
FLMFGYRLEE FPGRGVVEAL GEGLDVHEGD AALLARIFSV VRDGNTLVLH HENPKLDRES
CQILHEAVGR FSRDGISVEF LPTRGIAGIL LLRGDVLSAI TDSNPIAEGR PLMQVLPLRS
KVEDPRARKT AEVLNAYLRW SHQTLSEHPL NKNRKEQGLP PINAVGTQRA GMLGRLPSFS
EKWGLKGLMI ASGAVYHGIG QVIGMDIRKV GDTNDPGRDL RERLERAHRA REYDFIHVHT
KVTDEAGHTR NPLIKKRVIE AVDSALDYAV EEIIPDDDVL FIVTADHSTA SSGTMIHTGE
SVPLVMTGKY VRRDDVRNFD EVSCAAGGLS LVRGKELMYL VLNFLDRGKL WGLMDSPDDQ
PFTPGRYSPL LVD
//
