PHSA_SALTY
ID PHSA_SALTY Reviewed; 758 AA.
AC P37600;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Thiosulfate reductase molybdopterin-containing subunit PhsA {ECO:0000305};
DE EC=1.8.5.5 {ECO:0000269|PubMed:22081391};
DE AltName: Full=Thiosulfate reductase subunit alpha {ECO:0000305};
DE Flags: Precursor;
GN Name=phsA {ECO:0000303|PubMed:7751291}; OrderedLocusNames=STM2065;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=7751291; DOI=10.1128/jb.177.10.2813-2820.1995;
RA Heinzinger N.K., Fujimoto S.Y., Clark M.A., Moreno M.S., Barrett E.L.;
RT "Sequence analysis of the phs operon in Salmonella typhimurium and the
RT contribution of thiosulfate reduction to anaerobic energy metabolism.";
RL J. Bacteriol. 177:2813-2820(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 691-758.
RC STRAIN=LT2;
RX PubMed=7737516; DOI=10.1016/0378-1119(94)00930-q;
RA Alami N., Hallenbeck P.C.;
RT "Cloning and characterization of a gene cluster, phsBCDEF, necessary for
RT the production of hydrogen sulfide from thiosulfate by Salmonella
RT typhimurium.";
RL Gene 156:53-57(1995).
RN [4]
RP FUNCTION.
RC STRAIN=LT2;
RX PubMed=3108233; DOI=10.1128/jb.169.6.2391-2397.1987;
RA Clark M.A., Barrett E.L.;
RT "The phs gene and hydrogen sulfide production by Salmonella typhimurium.";
RL J. Bacteriol. 169:2391-2397(1987).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=LT2;
RX PubMed=22081391; DOI=10.1128/jb.06014-11;
RA Stoffels L., Krehenbrink M., Berks B.C., Unden G.;
RT "Thiosulfate reduction in Salmonella enterica is driven by the proton
RT motive force.";
RL J. Bacteriol. 194:475-485(2012).
CC -!- FUNCTION: Component of the PhsABC thiosulfate reductase that catalyzes
CC the reduction of thiosulfate to sulfite and hydrogen sulfide, with
CC menaquinol as the sole electron donor. Proton motive force (PMF) is
CC required to drive transmembrane electron transfer within the reductase.
CC The PhsA subunit contains the active site molybdenum-bis(molybdopterin
CC guanine dinucleotide) (Mo-bis-MGD) cofactor.
CC {ECO:0000269|PubMed:22081391, ECO:0000269|PubMed:3108233}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 2 H(+) + hydrogen sulfide + sulfite = a quinol +
CC thiosulfate; Xref=Rhea:RHEA:50736, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:24646, ChEBI:CHEBI:29919,
CC ChEBI:CHEBI:33542, ChEBI:CHEBI:132124; EC=1.8.5.5;
CC Evidence={ECO:0000269|PubMed:22081391};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P24183};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P24183};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250|UniProtKB:P24183};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:P24183};
CC -!- SUBUNIT: Composed of three subunits: PhsA, PhsB and PhsC.
CC {ECO:0000305|PubMed:22081391}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:22081391}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L32188; AAC36934.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20969.1; -; Genomic_DNA.
DR EMBL; L31538; AAA68431.1; -; Genomic_DNA.
DR PIR; A57143; A57143.
DR RefSeq; NP_461010.1; NC_003197.2.
DR RefSeq; WP_000028228.1; NC_003197.2.
DR AlphaFoldDB; P37600; -.
DR SMR; P37600; -.
DR STRING; 99287.STM2065; -.
DR TCDB; 5.A.3.5.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR PaxDb; P37600; -.
DR PRIDE; P37600; -.
DR EnsemblBacteria; AAL20969; AAL20969; STM2065.
DR GeneID; 1253586; -.
DR KEGG; stm:STM2065; -.
DR PATRIC; fig|99287.12.peg.2187; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; ASICEMC; -.
DR PhylomeDB; P37600; -.
DR BioCyc; MetaCyc:MON-12529; -.
DR BioCyc; SENT99287:STM2065-MON; -.
DR BRENDA; 1.8.5.5; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IBA:GO_Central.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
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; SSF50692; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..30
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 31..758
FT /note="Thiosulfate reductase molybdopterin-containing
FT subunit PhsA"
FT /id="PRO_0000019167"
FT DOMAIN 41..97
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 758 AA; 82800 MW; 46836316A6D08330 CRC64;
MSISRRSFLQ GVGIGCSACA LGAFPPGALA RNPIAGINGK TTLTPSLCEM CSFRCPIQAQ
VVNNKTVFIQ GNPSAPQQGT RICARGGSGV SLVNDPQRIV KPMKRTGPRG DGEWQVISWQ
QAYQEIAAKM NAIKAQHGPE SVAFSSKSGS LSSHLFHLAT AFGSPNTFTH ASTCPAGKAI
AAKVMMGGDL AMDIANTRYL VSFGHNLYEG IEVADTHELM TAQEKGAKMV SFDPRLSIFS
SKADEWHAIR PGGDLAVLLA MCHVMIDEQL YDASFVERYT SGFEQLAQAV KETTPEWAAA
QADVPADVIV RVTRELAACA PHAIVSPGHR ATFSQEEIDM RRMIFTLNVL LGNIEREGGL
YQKKNASVYN KLAGEKVAPT LAKLNIKNMP KPTAQRIDLV APQFKYIAAG GGVVQSIIDS
ALTQKPYPIK AWIMSRHNPF QTVTCRSDLV KTVEQLDLVV SCDVYLSESA AYADYLLPEC
TYLERDEEVS DMSGLHPAYA LRQQVVEPIG EARPSWQIWK ELGEQLGLGQ YYPWQDMQTR
QLYQLNGDHA LAKELRQKGY LEWGVPLLLR EPESVRQFTA RYPGAIATDS DNTYGEQLRF
KSPSGKIELY SATLEELLPG YGVPRVRDFA LKKENELYFI QGKVAVHTNG ATQYVPLLSE
LMWDNAVWVH PQTAQEKGIK TGDEIWLENA TGKEKGKALV TPGIRPDTLF VYMGFGAKAG
AKTAATTHGI HCGNLLPHVT SPVSGTVVHT AGVTLSRA
