ID A0A0U1NLA5_9RHOB Unreviewed; 940 AA.
AC A0A0U1NLA5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Sulfur reductase chain A {ECO:0000313|EMBL:CRK75505.1};
GN Name=psrA {ECO:0000313|EMBL:CRK75505.1};
GN ORFNames=NIG5292_01553 {ECO:0000313|EMBL:CRK75505.1};
OS Nereida ignava.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Nereida.
OX NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK75505.1, ECO:0000313|Proteomes:UP000048949};
RN [1] {ECO:0000313|EMBL:CRK75505.1, ECO:0000313|Proteomes:UP000048949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK75505.1,
RC ECO:0000313|Proteomes:UP000048949};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CVQV01000006; CRK75505.1; -; Genomic_DNA.
DR RefSeq; WP_048598923.1; NZ_CVQV01000006.1.
DR AlphaFoldDB; A0A0U1NLA5; -.
DR STRING; 282199.GCA_001049735_01552; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000048949; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02783; MopB_CT_2; 1.
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; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000048949}.
FT DOMAIN 16..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 916..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 940 AA; 104274 MW; 22E5499E250D9609 CRC64;
MGFNQPVVDT SPKVSDEVRK TTCYMCACRC GINVHMKEGK VAYIEGNKDH PVNQGVLCAK
GSAGIMQVNA PSRLRAPMKR VGERGSGEFE EITWEEAYDI AVSKLKPIRD EDPSKLAFFT
GRDQSQSFTS LWAQGFGTPN YAAHGGFCSV NMAAAGIYTM GGAFWEFGQP DWDHTKMLMI
FGVAEDHDSN PIKMGLGKIK ARGAKVVGVN PIRSGYNAVA DEWVGITPGT DGLFILSMLH
CLIKAGKIDL DYLSQFTNAP VLLDETDGSA EEGLFLKDKD GKALVIDRNT GKLAPFDGKG
VYPDLAGTHR KAGVTHRTVF HHMIERYMSE EYAPEAVAER CGISAKRIRK LAAELADVAF
NQAIELDRPW TDFRGKKHDK MVGRPVSFHS MRGISAHANG FQTCRALHVL QIMLGSVETP
GGMRFKPPYP KPATAHPKPH CKVTPGAALD GPHLGFTHGP DDLCLREDGT AARIDKAFTW
ENPMSSHGMM HMVISNAHAG DPYKIDTLFM YMANMSWNSS MNTSGVIEML TDKDEDGNYV
IPNIIYSDAY SSEMVAYSDL ILPDTTYLER HDCISLLDRP ICEADAVADA IRWPVVEPDR
DVKGFQSALC DLGARLGLPG FVNEDGSQKY EDYADYITNH IRRPGVGPLA GWRVGEDGLQ
GGRGDVNEAQ LDAYIENGGF WMEHVPEDAA YYKPFNMGYQ DWAVKMGFFD AVQPYIFQLY
VEPMRKFQLA AEGHGERQPP EHLRERIKHT LDPLPIWYSN EPENLADQYP VTALTQRPMA
MYHSWGSQNA WLRQIHGHNP LYVPTKIWEE NSFEEGDWAK VVSPHGEIVV PVAHMAALND
NTVWTWNAIG KRKGAWALEE NAPETTKGFL LNHLIHELLP ANGDGMRWAN SDPITGQAAW
FDLKVRIEKS DVAGQTLPDF APQKSPVGKG PKDLAWKLGK
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