TTRA_ARCFU
ID TTRA_ARCFU Reviewed; 1134 AA.
AC O30078;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Tetrathionate reductase subunit A;
DE EC=1.8.-.-;
DE AltName: Full=Tetrathionate reductase molybdenum subunit;
DE Flags: Precursor;
GN Name=ttrA; OrderedLocusNames=AF_0159;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP INTERACTION WITH TTRD, EXPORT VIA THE TAT-SYSTEM, DOMAIN, GENE NAME, AND
RP MUTAGENESIS OF ARG-6; VAL-15; SER-17; VAL-20; LEU-22 AND GLY-24.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=22289056; DOI=10.1021/bi201852d;
RA Coulthurst S.J., Dawson A., Hunter W.N., Sargent F.;
RT "Conserved signal peptide recognition systems across the prokaryotic
RT domains.";
RL Biochemistry 51:1678-1686(2012).
CC -!- FUNCTION: Part of a membrane-bound tetrathionate reductase that
CC catalyzes the reduction of tetrathionate to thiosulfate. TtrA is the
CC catalytic subunit (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBUNIT: Probably composed of three subunits: TtrA, TtrB and TtrC (By
CC similarity). Precursor interacts with TtrD. {ECO:0000250,
CC ECO:0000269|PubMed:22289056}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: Residues 7-17 are sufficient for TtrD recognition.
CC {ECO:0000269|PubMed:22289056}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE000782; AAB91069.1; -; Genomic_DNA.
DR PIR; G69269; G69269.
DR RefSeq; WP_010877671.1; NC_000917.1.
DR AlphaFoldDB; O30078; -.
DR STRING; 224325.AF_0159; -.
DR EnsemblBacteria; AAB91069; AAB91069; AF_0159.
DR GeneID; 24793710; -.
DR KEGG; afu:AF_0159; -.
DR eggNOG; arCOG01491; Archaea.
DR eggNOG; arCOG01496; Archaea.
DR HOGENOM; CLU_008235_0_0_2; -.
DR OMA; ERYSGCP; -.
DR OrthoDB; 1029at2157; -.
DR PhylomeDB; O30078; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR CDD; cd02758; MopB_Tetrathionate-Ra; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037946; MopB_CT_Tetrathionate.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR041929; Tetrathionate-R_A_N.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 32..1134
FT /note="Tetrathionate reductase subunit A"
FT /id="PRO_0000417415"
FT DOMAIN 46..133
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 119
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT MUTAGEN 6
FT /note="R->Q: Does not affect TtrD binding."
FT /evidence="ECO:0000269|PubMed:22289056"
FT MUTAGEN 15
FT /note="V->Q: Strong decrease in TtrD binding."
FT /evidence="ECO:0000269|PubMed:22289056"
FT MUTAGEN 17
FT /note="S->Q: Does not affect TtrD binding."
FT /evidence="ECO:0000269|PubMed:22289056"
FT MUTAGEN 20
FT /note="V->Q: Does not affect TtrD binding."
FT /evidence="ECO:0000269|PubMed:22289056"
FT MUTAGEN 22
FT /note="L->Q: Does not affect TtrD binding."
FT /evidence="ECO:0000269|PubMed:22289056"
FT MUTAGEN 24
FT /note="G->Q: Does not affect TtrD binding."
FT /evidence="ECO:0000269|PubMed:22289056"
SQ SEQUENCE 1134 AA; 127689 MW; D256217AF51A9C87 CRC64;
MQLSRRDFIK GLVAVGSASV FLAGYSETVD RLVKPRYTEV KPDSVGRIVH SACLGCNVRC
GIRVNVVQRG GMEVVERISG NPYHVYNRYV SKEKQSRRYE PLPYNTPITE GLKYSGTLCA
RGEDGIHYLY DPYRIIVPLK RAGPRGSGKF KPITWEQLIN EVVNGGVIEE TGERLPGLKE
LFAYGILSEA GFDANAVLSE MKKDVDAIME IAKDDTKSYG ELTEAINNFK AKWSAKLGEK
GLKLEDILID PDRPDLGTKA NQLVYMRGRG QGHADYFYQR WTYAFGSVNW LRHTSSCQLG
YYAGNKIWSG YHDVQADPIG AKLLLMVGAQ MGRLHPGATG QGLIVERAAE GELKVYYVNP
TAPRTTANGN IVWVPIRPGT DAAFAMALLR VMFERGYYDA EFLSYANTDA ARKAGYPLNT
NASWLVIWEG DRKGEFLKGE DIGLGSDNPV VYAGSFVTND SVEKAEIFFD GYVETKEGKR
RVKSALQILK EECFSRSVEE WCEICGVDVA VIYEIAEEIR KAMPNCGTIV HRGAGMHTNG
EYNVWALRCI DMLIGNIHRK GGLMTRASHT NYNKELYYVD KSKFGEPVRW GPPIDRHKVA
YEDSLEYWMK KKRGENPYPA KRPWYPLTPE ESYTEMFAGI AEEYPYPIKA LIMYYANPVL
SANFGVKFIE VLKDTSKLPL FIAITTSINE TFLYADYIVP DTMYLETGTM GINYLYATSA
SVTLAEYWRS PAVMPMTQLV GTCPNGHPKY ASMWEFLIDI ALKLKMPGYG KGAVKGVGAY
DGQKFDLYCA WEYIMYVFAN AAMDAKKRGL IPETVSDEEV DFVEKNYPIA RFKDIVPNEW
RYVAYGLARG GVFTRYEDSF DERGYSKRKP WTDTVYFWSE KLAKARNSVT GEKFYGGPKY
LPPATYAPLG TERRFYGTPL REIYPESQYP FLVVPPGSPL FTKHRSMFYY WLKQVMPENF
AVINPEDAEK LGIESGDVIK IVTPTGELEV VAAVEPTVVK GTIAIPVGMG RWADSAVKKP
AYFRLNDGSV AALVSELPDG ASLPSDAVNP VKQLDETKKR ILFTKSDRRY YDDLGIDSWR
FSGVTPNVVA CVDTSLDNWP LLSWIGAAQV YFFIPAKVEK TGKRKKFEMP NVWW
