PPAX_CALS4
ID PPAX_CALS4 Reviewed; 220 AA.
AC Q8R821;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Putative pyrophosphatase PpaX {ECO:0000255|HAMAP-Rule:MF_01250};
DE EC=3.6.1.1 {ECO:0000255|HAMAP-Rule:MF_01250};
GN Name=ppaX {ECO:0000255|HAMAP-Rule:MF_01250}; OrderedLocusNames=TTE2216;
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01250};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PpaX family.
CC {ECO:0000255|HAMAP-Rule:MF_01250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM25368.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008691; AAM25368.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041587361.1; NC_003869.1.
DR AlphaFoldDB; Q8R821; -.
DR SMR; Q8R821; -.
DR STRING; 273068.TTE2216; -.
DR PRIDE; Q8R821; -.
DR EnsemblBacteria; AAM25368; AAM25368; TTE2216.
DR KEGG; tte:TTE2216; -.
DR eggNOG; COG0546; Bacteria.
DR HOGENOM; CLU_045011_19_3_9; -.
DR OMA; LLIFDWD; -.
DR Proteomes; UP000000555; Chromosome.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01250; Pyrophosphat_PpaX; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR023733; Pyrophosphatase_Ppax.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..220
FT /note="Putative pyrophosphatase PpaX"
FT /id="PRO_0000056845"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01250"
SQ SEQUENCE 220 AA; 25682 MW; A4FEE7C7BF5058C6 CRC64;
MKITAVLFDL DGTIIDTNQL IIKSFVYTVE KHLGYKIGAE EVIPYFGEPL PLTLQRFSKD
KWEIMLKTYR DYNEKYHDRY TKIREDVKEV LARLKEEGIK TAVVTSKRRE LAKRGLKLFE
LDKYFDVLVG LEDTEKHKPE PDPVLKALEL LKSPREEALM VGDSPYDILS ARSAGVRSVA
VKWSVLPFEL LKKEKPDYFI EDMWQLLKII KGCDEDEHEQ
