TTH_ACIF2
ID TTH_ACIF2 Reviewed; 499 AA.
AC B7J3C9; Q0KK37;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Tetrathionate hydrolase {ECO:0000303|PubMed:17904676};
DE Short=4THase {ECO:0000303|PubMed:17904676};
DE Short=TTH {ECO:0000250|UniProtKB:G8YXZ9};
DE EC=3.12.1.- {ECO:0000269|PubMed:17904676, ECO:0000269|PubMed:25144400};
DE Flags: Precursor;
GN Name=tth {ECO:0000303|PubMed:17904676};
GN Synonyms=tetH {ECO:0000312|EMBL:ACK80599.1};
GN OrderedLocusNames=AFE_0029 {ECO:0000312|EMBL:ACK80599.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-45, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=17904676; DOI=10.1016/j.jbiotec.2007.08.030;
RA Kanao T., Kamimura K., Sugio T.;
RT "Identification of a gene encoding a tetrathionate hydrolase in
RT Acidithiobacillus ferrooxidans.";
RL J. Biotechnol. 132:16-22(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF CYS-301.
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=25144400; DOI=10.1080/09168451.2014.948374;
RA Kanao T., Nakayama H., Kato M., Kamimura K.;
RT "The sole cysteine residue (Cys301) of tetrathionate hydrolase from
RT Acidithiobacillus ferrooxidans does not play a role in enzyme activity.";
RL Biosci. Biotechnol. Biochem. 78:2030-2035(2014).
RN [4]
RP CRYSTALLIZATION.
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=23722856; DOI=10.1107/s1744309113013419;
RA Kanao T., Kosaka M., Yoshida K., Nakayama H., Tamada T., Kuroki R.,
RA Yamada H., Takada J., Kamimura K.;
RT "Crystallization and preliminary X-ray diffraction analysis of
RT tetrathionate hydrolase from Acidithiobacillus ferrooxidans.";
RL Acta Crystallogr. F 69:692-694(2013).
CC -!- FUNCTION: Catalyzes the hydrolysis of tetrathionate to generate
CC elemental sulfur, thiosulfate and sulfate.
CC {ECO:0000269|PubMed:17904676, ECO:0000269|PubMed:25144400}.
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:17904676,
CC ECO:0000269|PubMed:25144400};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.0. {ECO:0000269|PubMed:17904676};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:17904676};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17904676,
CC ECO:0000269|PubMed:25144400}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17904676}.
CC Note=Membrane-associated. {ECO:0000269|PubMed:17904676}.
CC -!- SIMILARITY: Belongs to the tetrathionate hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AB259312; BAF03501.1; -; Genomic_DNA.
DR EMBL; CP001219; ACK80599.1; -; Genomic_DNA.
DR RefSeq; WP_012535754.1; NC_011761.1.
DR PDB; 6L8A; X-ray; 1.95 A; A/B/C/D/E/F=33-499.
DR PDB; 7CQY; X-ray; 2.80 A; A/B/C/D/E/F=33-499.
DR PDBsum; 6L8A; -.
DR PDBsum; 7CQY; -.
DR AlphaFoldDB; B7J3C9; -.
DR SMR; B7J3C9; -.
DR STRING; 243159.AFE_0029; -.
DR PaxDb; B7J3C9; -.
DR EnsemblBacteria; ACK80599; ACK80599; AFE_0029.
DR GeneID; 66431023; -.
DR KEGG; afr:AFE_0029; -.
DR eggNOG; COG1520; Bacteria.
DR HOGENOM; CLU_030956_0_0_6; -.
DR OMA; ANFVHYE; -.
DR OrthoDB; 1377603at2; -.
DR BioCyc; MetaCyc:MON-15073; -.
DR BRENDA; 3.12.1.B1; 91.
DR Proteomes; UP000001362; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
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; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF50998; SSF50998; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Hydrolase;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:17904676"
FT CHAIN 33..499
FT /note="Tetrathionate hydrolase"
FT /id="PRO_5002854957"
FT MUTAGEN 301
FT /note="C->A: No change in activity. Does not affect
FT dimerization."
FT /evidence="ECO:0000269|PubMed:25144400"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:7CQY"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 423..427
FT /evidence="ECO:0007829|PDB:7CQY"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:6L8A"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:6L8A"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:6L8A"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:6L8A"
SQ SEQUENCE 499 AA; 53133 MW; 8ED27450E2E31FE7 CRC64;
MPSIVRNHGP HNKILLSALL LALFGWVPLA SAAVAVPMDS TGPYRTVSHP ENAPSGVDAG
VGPSEWTHAY ANPAHNAAFP VPDDAPEWIR NGVSWLFPEA RAWPLANPPF GSKTYGAAEA
SVTQTQFYGN ALGPSVVDGV VYAESDDMFA YAVNAKTGKL IWRASPVGNN LMGNPLVIGN
TVYLSAGSVA FNFANVLRYA HNPSASARGL NVSFNGIYAL NRSNGKLLWY FATPGETMAT
PAYDNNTLFI ADGAGNAFGI NATTGKQVWK THVGGMDNMS SVTAYRHNIY FAMAIKPYLY
CLNESNGHIV WKGTIPGASN TGIGDVSPAA ADGVVVLDAT TKPQANKKAM FSNVIRAFDA
KTGAVLWTRN MGSGGKIPAF KGGVPMIHNN IVYVGNPVAS TYQAYELKTG KLLWTWHVPT
KVAAGAGRSA PTYYKGLLYI TTGQYIFVVN PATGKELHQH HIGGQFGIES PVIVGGTVYL
TNSWDWIMAI PLKTISHGS
