ID A0A0J1I9H0_9FIRM Unreviewed; 832 AA.
AC A0A0J1I9H0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Polysulfide reductase chain A {ECO:0000313|EMBL:KLU61281.1};
GN Name=psrA_3 {ECO:0000313|EMBL:KLU61281.1};
GN ORFNames=CEB3_c25010 {ECO:0000313|EMBL:KLU61281.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU61281.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU61281.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU61281.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLU61281.1}.
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DR EMBL; LDXJ01000056; KLU61281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1I9H0; -.
DR STRING; 999898.CEB3_c25010; -.
DR PATRIC; fig|999898.3.peg.2788; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000035957; Unassembled WGS sequence.
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:InterPro.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 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 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000035957}.
FT DOMAIN 11..67
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 832 AA; 93430 MW; 284424AB10C16014 CRC64;
MRQAELTAQK DYWAKSACKM CIHSCAIRVH VVDGVVLKIE GDPENENNKG KLCPKGQAGI
MRLYDPNRVK TPLKRTNPKK GIGVDPKWEA ISWEEAYEIT AKKLKKIRDE DPRKLLVSIN
DFHRIHLWGW GSAFGSANYF STVGQYCGAA YHPVNGSLDG SFAATNDYEY CNYWIQIGGG
DGFSSHLHVA GSIKRMAEAR VNRGMKVVVV EPRMSTGAAK ADEWIPILPG TDRAFVLGMV
NVLLHELNVY DAGFLKKHTN GPYLIGPDGK FVRDRETGKA LVWDAGSDSA KDYDDESIRE
FSLEGNYTVN GVKCQPGFQV IKDTLKDHTP ERMSKICTVP AETIRRIARE YGEAARIGST
IVIEGKEYPY RPAAVNYYRG AIGHVDGGLD SSAMKLINLI VGNIDVPGGH IGVGLDHRLL
LVEPGSDGMI KPQPHILHPP YAFADKPYSF QLMEWFPIGI DPGHLSADNI LNPEKYGFDF
KAEALIIEHS NPMWNLSATD EVTEVFKKLD FIVAIDVVLN ESSEWADIVF PDHTYLESHL
LVDIEPPVIT GHVYRRPVIE PLYDSRDATD ILTELAARIG FLEQWNGLLN FTAFLKPEYY
LEPNKKYTNL EITDRMAKSI YGPDHGLDWF QENGHAVRHQ TPEEMYLPYR GLRIPVYFNF
FKETGEDLQA KMTAAGRKWD TSSYLPVPVW RDSHPLHNIP PEYDLYAFAF KETLLNFSES
NSVPWINEAM EHIPMHMGVM INTKTAKAKG IKTGDMLRIT SPFGEITGRA SVVEEIHPGC
IAMSNGISRW SNHPIPKKSN THFNRLLPAD VKWTDGMTGH LETSTKVKIA KI
//
