ID A0A2T0AQN9_9FIRM Unreviewed; 723 AA.
AC A0A2T0AQN9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 02-APR-2025, entry version 33.
DE SubName: Full=Polysulfide reductase chain A {ECO:0000313|EMBL:PRR71240.1};
GN Name=psrA_2 {ECO:0000313|EMBL:PRR71240.1};
GN ORFNames=MOHU_16660 {ECO:0000313|EMBL:PRR71240.1};
OS Moorella humiferrea.
OC Bacteria; Bacillati; Bacillota; Clostridia; Moorellales; Moorellaceae;
OC Moorella.
OX NCBI_TaxID=676965 {ECO:0000313|EMBL:PRR71240.1, ECO:0000313|Proteomes:UP000238415};
RN [1] {ECO:0000313|EMBL:PRR71240.1, ECO:0000313|Proteomes:UP000238415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23265 {ECO:0000313|EMBL:PRR71240.1,
RC ECO:0000313|Proteomes:UP000238415};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Moorella humiferrea DSM 23265.";
RL Submitted (MAR-2018) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:PRR71240.1}.
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DR EMBL; PVXM01000043; PRR71240.1; -; Genomic_DNA.
DR RefSeq; WP_106005623.1; NZ_CP136419.1.
DR AlphaFoldDB; A0A2T0AQN9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000238415; Unassembled WGS sequence.
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; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR050612; Prok_Mopterin_Oxidored.
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 Pfam; PF10518; TAT_signal; 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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 Reference proteome {ECO:0000313|Proteomes:UP000238415};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 45..101
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 723 AA; 77573 MW; 0F94E09C5D125C9B CRC64;
MLEQKISRRT FIKGSLVAGA VAAFGGSLVP LKGAEAAEAP EASATKVVPT ICEMCGVKCG
VLAHVKDGRV WRLTGNPKDP QSGGRLCARG NAGTKTLYDP DRLKGPLKRV GDGKFEPISW
EQAFKEIGEK LIELKGRYGP QTLVWLAHPE LISPLEKHFM AAFGSPNYTG HGPTCYSSRN
VAFEQMYGGV PGVDYRNIKY YIAFGRNLTG GIKNPDIQKI VAAKAEGAHL VAVDPRFNDF
AYFADEWLPI RPGTDLAMIL AMINVIIREN LYDASFVAER TVGFEELKAG VASYTPEWAA
QITGIDAATI ARIARELAAA KPAAAVDPGW HAVTGSQYYN SVQTARAVAA LNALLGNLGA
KGGLSFPPTI KFGDPGPLMG PKPPAAVAPR WDGAGGEKWP LNKAHGIIQI FPERVKEDKP
YPVKAVVIQH LNPVRSSTNS AAFIEALKQL ELVVAIDIQM NDTAYYAHYV LPEATYLERY
DPLMTAGNKV ILRQPAVQPL FDTKGAEEII GGIAKAAGLG EYFNFTLEQY NDAMLAPLGL
TQAELARTGV AEVAAQPPDY TKLKTPSGKI ELACQAFVKA GSTLTPAWEP PLVEPKENEF
RFIQGHVPMH THTTTDNNAY LHALMPENEL WINPARAAKL GIKTGDVVEV TSKVGSVKVK
ARVTECIHPE AVFLAHGFGC GVPLRKLAYN SGANGGALIP IITAPVSGAA AQCETLVTVR
KAG
//
