ID B4EZI1_PROMH Unreviewed; 759 AA.
AC B4EZI1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Thiosulfate reductase {ECO:0000313|EMBL:CAR43771.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CAR43771.1};
GN Name=phsA {ECO:0000313|EMBL:CAR43771.1};
GN OrderedLocusNames=PMI1814 {ECO:0000313|EMBL:CAR43771.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR43771.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR43771.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR43771.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AM942759; CAR43771.1; -; Genomic_DNA.
DR RefSeq; WP_012368115.1; NC_010554.1.
DR AlphaFoldDB; B4EZI1; -.
DR EnsemblBacteria; CAR43771; CAR43771; PMI1814.
DR GeneID; 6801043; -.
DR KEGG; pmr:PMI1814; -.
DR PATRIC; fig|529507.6.peg.1763; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000008319; Chromosome.
DR GO; GO:0051536; F:iron-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; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR CDD; cd02755; MopB_Thiosulfate-R-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAR43771.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 41..97
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 759 AA; 83834 MW; 0A7FC42A5574BFC4 CRC64;
MSISRRSFIK GMGIGCVGCT VGSLPPGALA LNPVTSLKGQ SKLTPSLCEM CSYRCPIEAQ
VVNNKTVFIQ GNRNSPHQKT RVCARGGSGV SLIYDPKRIV KPMKRKGPRG AGEWEVISWE
QAYTEIAEKM ASIKQHYGAE SIFFSSKSGS LSSHLFHLAA AFGSPNTFTH ASTCPAGKAI
AASVMMGGDL KMDLANSKYI LSFGHNLYEG IEVAETYELM TAQERGAKLV SFDPRLSVVS
SKANEWFAIR PGGDLPVLMA MCHIMVKENL YDKDFIEKFT VGFPQLVEVL QDTTPEWAQA
HSDVPAKDII RITREIAAKA PHALVMPGHR ATFNKDEINM RRMIFTFNAL LGNIEREGGM
YQKKAAAKYN KLAGIDVAPE LAKPTVKGMP KITAKRVDAT APQFKYINKG GGIVQSIIDS
TLHGVPYQTK AWIMSRHNPF QTVSCRPDLE KTAQKLDLIV SCDVYLSESA SYADYLLPES
TYLERDEEIS DVSGLNPAYA LRQQVVEPIG DTKPSWLIWM ELGKKLGLAS YYPWENMGVR
QLYQVKGDEN LYKEIHQKGY LSYGIPLLLR EPSYVKAFVA QYPDAIKHVD SNNMMEKSLS
FKSPSGLIEI YSEELESLLE NYGIPRFHNF PLKQKDELYF IQGKVAVHTN GATQYVPLLA
ELMWKNPVWL HPDTAKSHGI KHGDEIILEN SVGKEKAHAL ITTGIRPDTV FVYMGSGSKT
GEKTPATTNG IHCSSLLPHE ISPVSGTDVH TSGVKISLA
//
