ID S5ZE77_9CREN Unreviewed; 424 AA.
AC S5ZE77;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Phosphonopyruvate decarboxylase {ECO:0000313|EMBL:AGT35393.1};
GN ORFNames=N186_05235 {ECO:0000313|EMBL:AGT35393.1};
OS Thermofilum adornatum.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=1365176 {ECO:0000313|EMBL:AGT35393.1, ECO:0000313|Proteomes:UP000015543};
RN [1] {ECO:0000313|EMBL:AGT35393.1, ECO:0000313|Proteomes:UP000015543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1910b {ECO:0000313|Proteomes:UP000015543};
RX PubMed=24029764;
RA Dominova I.N., Kublanov I.V., Podosokorskaya O.A., Derbikova K.S.,
RA Patrushev M.V., Toshchakov S.V.;
RT "Complete Genomic Sequence of 'Thermofilum adornatus' Strain 1910bT, a
RT Hyperthermophilic Anaerobic Organotrophic Crenarchaeon.";
RL Genome Announc. 1:e00726-13(2013).
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; CP006646; AGT35393.1; -; Genomic_DNA.
DR RefSeq; WP_020962699.1; NC_022093.1.
DR AlphaFoldDB; S5ZE77; -.
DR GeneID; 25405574; -.
DR KEGG; thb:N186_05235; -.
DR PATRIC; fig|1365176.7.peg.1035; -.
DR eggNOG; arCOG01696; Archaea.
DR HOGENOM; CLU_034906_2_0_2; -.
DR OrthoDB; 52918at2157; -.
DR Proteomes; UP000015543; 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; 1.
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 Pyruvate {ECO:0000313|EMBL:AGT35393.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015543}.
FT DOMAIN 1..405
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 424 AA; 46931 MW; 7AF05A686D7EC853 CRC64;
MKLIYLVLDG VADKPEDGPT SLELANKPFL DKVASLSRCG LMYTVGKGIA PESDAAVMSI
LGYDPHKEYT GRGPVEAVGA GLELREGYEV AFRANFATID PKTRKILDRR CGRNLSSEEA
HELAKAVDGL ELGVYDGYAR VVATVGHRAV VIIGSKTHRV SDNVSNTDPA YEKHGYVSIA
KSSFEPYVAE AKPLDGTEEA RIMATLVNKF TEKIIQILKD HPINQERIKN GKMPANVILL
RDSGGRLPRL EEINKKFGLR FGAVAEMPVE IGIARILKMD MESVPPPTED KAVDYKIRLE
ATMKLLERND VVYVHLKGPD EPGHDGDVKR KVESIELIDR YYVGPLLEQI SGKEIALLVT
ADHATPYTRK SHTDDPVPVV LMLPRNKQDG LKRLTEKECS RGSLGVFQHG YELLPRILEM
IKSP
//
