TTH_ACIAM
ID TTH_ACIAM Reviewed; 535 AA.
AC G8YXZ9;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Tetrathionate hydrolase {ECO:0000303|PubMed:21747790};
DE Short=4THase {ECO:0000250|UniProtKB:B7J3C9};
DE Short=TTH {ECO:0000303|PubMed:21747790};
DE EC=3.12.1.- {ECO:0000269|PubMed:21747790};
DE Flags: Precursor;
GN Name=tth1 {ECO:0000303|PubMed:21747790};
OS Acidianus ambivalens (Desulfurolobus ambivalens).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Acidianus.
OX NCBI_TaxID=2283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-53, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR
RP LOCATION, INDUCTION, AND GLYCOSYLATION AT ASN-50.
RC STRAIN=Lei 10 / DSM 3772 / JCM 9191;
RX PubMed=21747790; DOI=10.3389/fmicb.2011.00068;
RA Protze J., Mueller F., Lauber K., Nass B., Mentele R., Lottspeich F.,
RA Kletzin A.;
RT "An extracellular tetrathionate hydrolase from the thermoacidophilic
RT archaeon Acidianus ambivalens with an activity optimum at pH 1.";
RL Front. Microbiol. 2:68-68(2011).
CC -!- FUNCTION: Catalyzes the hydrolysis of tetrathionate to generate
CC elemental sulfur, thiosulfate and sulfate.
CC {ECO:0000269|PubMed:21747790}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetrathionate = H(+) + sulfate + sulfur + thiosulfate;
CC Xref=Rhea:RHEA:13541, ChEBI:CHEBI:15226, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:26833,
CC ChEBI:CHEBI:33542; Evidence={ECO:0000269|PubMed:21747790};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for tetrathionate (at pH 1 and 80 degrees Celsius)
CC {ECO:0000269|PubMed:21747790};
CC pH dependence:
CC Optimum pH is 1. No activity is detected at pH 6.
CC {ECO:0000269|PubMed:21747790};
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.
CC {ECO:0000269|PubMed:21747790};
CC -!- SUBUNIT: Monomer and homodimer; in equilibrium.
CC {ECO:0000269|PubMed:21747790}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:21747790}.
CC Note=Associated with the S-layer in the pseudo-periplasmic space.
CC {ECO:0000269|PubMed:21747790}.
CC -!- INDUCTION: Expressed in tetrathionate-grown cells.
CC {ECO:0000269|PubMed:21747790}.
CC -!- SIMILARITY: Belongs to the tetrathionate hydrolase family.
CC {ECO:0000305}.
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DR EMBL; FR734215; CBY66038.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YXZ9; -.
DR SMR; G8YXZ9; -.
DR iPTMnet; G8YXZ9; -.
DR BRENDA; 3.12.1.B1; 86.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:21747790"
FT CHAIN 40..535
FT /note="Tetrathionate hydrolase"
FT /id="PRO_0000444002"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21747790"
SQ SEQUENCE 535 AA; 57659 MW; F3E798AE92B19E82 CRC64;
MNLKILVGLF ILGIIILSAM TFLNFTTIVA QDKGDQQPKG PIVYTYTEYN GTYFPHILTV
VYYPCNATCS NLGFPSVWPV SNENQCHNAV VNTTCQALIE GVDWQLPLLN YVGGVAIPLS
TPPCKLPWAQ QLGVKGALVY YTQMVGEPLG VTLACGLLYA TEDSMPGSIT AINPVTGKIV
WMANGLAGPA MNNPVVWHGI VYVSVGGVCF TFSQFVHFED HQYCKIHRGR CGAVYAFNAT
NGQLLWMRFT YGEAMPAPAI YDGILAYVTG GGCFVGVNAT TGQTLWVDHF PGFIANMASV
NYYVLPNGTP LFIAGFTYTA PPYGYIIAVN GLNGHEAWNA TMPAPYVGAN TGLGDVAPAV
DQQLGIVVDN DIANFSNGYV DMVTFALNAT NGKPLWAVNT GRGPIPPAYK GGMPLIVGNV
VYDGNPSLGT VNAICIKTGK ILWSTKLPCL QTPPKFPGGP RGSPTYYHGL LWVSAGQYVY
VINPKNGDIL TFYWIGGRLG IMNPVIAGNT MFLSNSYGWI VAIPLSQIYP AYIYY