PSRA_WOLSU
ID PSRA_WOLSU Reviewed; 763 AA.
AC P31075;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Polysulfide reductase chain A;
DE AltName: Full=Sulfur reductase chain A;
DE Flags: Precursor;
GN Name=psrA; OrderedLocusNames=WS0116;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-52.
RX PubMed=1597189; DOI=10.1111/j.1432-1033.1992.tb16953.x;
RA Krafft T., Bokranz M., Klimmek O., Schroeder I., Fahrenholz F., Kojro E.,
RA Kroeger A.;
RT "Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes
RT polysulphide reductase.";
RL Eur. J. Biochem. 206:503-510(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- FUNCTION: Component of the phosphorylative electron transport system
CC with polysulfide as the terminal acceptor.
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: Functional polysulfide reductase is made up of three different
CC (A, B, and C) subunits.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE09281.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X65042; CAA46176.1; -; Genomic_DNA.
DR EMBL; BX571657; CAE09281.1; ALT_INIT; Genomic_DNA.
DR PIR; S23457; S23457.
DR AlphaFoldDB; P31075; -.
DR SMR; P31075; -.
DR STRING; 273121.WS0116; -.
DR TCDB; 5.A.3.5.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR EnsemblBacteria; CAE09281; CAE09281; WS0116.
DR KEGG; wsu:WS0116; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR OrthoDB; 88184at2; -.
DR BioCyc; MetaCyc:MON-12581; -.
DR Proteomes; UP000000422; Chromosome.
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 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 Pfam; PF10518; TAT_signal; 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; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..34
FT /note="Tat-type signal"
FT CHAIN 35..763
FT /note="Polysulfide reductase chain A"
FT /id="PRO_0000019150"
FT DOMAIN 44..100
FT /note="4Fe-4S Mo/W bis-MGD-type"
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 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 763 AA; 84751 MW; 2460CFD93EDD5105 CRC64;
METTMTRRDF LKSAGAAGAA GLVWSQTIPG TLGALEKQEI KGSAKFVPSI CEMCTSSCTI
EARVEGDKGV FIRGNPKDKS RGGKVCARGG SGFNQLYDPQ RLVKPIMRVG ERGEGKWKEV
SWDEAYTFIA KKLDEIKQKH GAHTVAFTAR SGWNKTWFHH LAQAYGSPNI FGHESTCPLA
YNMAGRDVFG GSMNRDFAKA KYIINMGHNV FEGIVISYVR QYMEAIENGA KVVTLEPRLS
VMAQKASEWH AIKPGHDLPF VLGFMHTLIF ENLYDKKFVQ KYCTGFEELK ASIEPCTPEK
MALECDIPAD TIKRLAREFA KAAPKAIFDF GHRVTFTPQE LELRRAMMMV NALVGNIERD
GGMYFGKNAS FYNQFLGEED PKAKGLKKPK TPAYPKVEVP RIDRIGEKDG EFFLANKGEG
IVSLVPKATL NELPGVPCKI HGWFIVRNNP VMTQTNADTV IKALKSMDLV VCVDIQVSDT
AWFADVVLPD TTYLERDEEF TAGGGKNPSF GIGRQKVVEP LGDAKPGWKI AKELSEKMGL
GEYFPWKDIE DYRLQQVDGD LDLLAKLKKD GSASFGVPLM LQEKKSVAEF VKKFPGAASK
VNEEGLIDFP KKIQLFSPKL EEVSGKGGLG YEPFKYKEED ELYFVQGKTP VRSNSHTGNV
PWLNNLMEYD AIWIHPKTAS KLGIKNGDAI ELYNKFSSQK SKALITEGVR EDTLFGYFGF
GHVSKDLKRA YGKGVNSNAL MPSFTSPNSG MDLHVFGVKV KKA
