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Database: UniProt
Entry: A0A091ANI8_9GAMM
LinkDB: A0A091ANI8_9GAMM
Original site: A0A091ANI8_9GAMM 
ID   A0A091ANI8_9GAMM        Unreviewed;       948 AA.
AC   A0A091ANI8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN   ORFNames=N790_12225 {ECO:0000313|EMBL:KFN41753.1};
OS   Arenimonas malthae CC-JY-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1384054 {ECO:0000313|EMBL:KFN41753.1, ECO:0000313|Proteomes:UP000029392};
RN   [1] {ECO:0000313|EMBL:KFN41753.1, ECO:0000313|Proteomes:UP000029392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-JY-1 {ECO:0000313|EMBL:KFN41753.1,
RC   ECO:0000313|Proteomes:UP000029392};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas malthae.";
RL   Submitted (SEP-2013) 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}.
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:KFN41753.1}.
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DR   EMBL; AVCH01000215; KFN41753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091ANI8; -.
DR   STRING; 1384054.N790_12225; -.
DR   PATRIC; fig|1384054.3.peg.2731; -.
DR   eggNOG; COG0243; Bacteria.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000029392; 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: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; IPR006657; MoPterin_dinucl-bd_dom.
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   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   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}.
FT   DOMAIN          17..73
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          918..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  104877 MW;  2FA188E3E272A0D7 CRC64;
     MPAMREPDLD LQQPVGDQVR QTTCYMCACR CGINVHLRGD RVRYIEGNPA HPVNRGVLCA
     KGSAGILQHY SPARLDKPLL RVGERGENKF REIEWDEALA LAAGWLSEAR ERDPDRLAFF
     TGRDQSQALT GWWAQQYGTI NYAAHGGFCS VNMAAGGLYT LGGSFWEFGE PDWEHTKYLV
     LWGVAEDHDS NPIKLGLGQL KGRGAKVVAV NPVRSGYGAI ADEWIGIRPG TDGLFAFALI
     HELLKADRID LDYLVNFTNA HWLVVDNPGG ADDGLFARDA EGRPLCWNRD LASVGAAPAE
     GTGLNPAVVG EYTLPDGRRV RPAFHLVARR YLDPQYAPEA VAERCGVPAA TIRRIAAEIA
     AAAFDDPVVI EQPWTDMHGR RHERMVGRPV AFHAMRGISA HSNGFHTCRA LHLLQLLLGA
     VDTPGSFRYQ PPFPRPIPPA NRPGKSRQAD GALDAAPLGF VHGPEDLLVD ADGQPRRLDH
     AYSWRYPLAV HGMLHTVIRN AWAADPKPVD VLMLFMANMS WNSAMNTAET MHWLTDKGDD
     GQYRIPRIIY SDAYSSEMVA YADLVLPDTT YLERFDAISL LDRPISDAER AADALRHPVL
     DPATQREGRD VRGFQSVLLD LGARIGLPAL VDDDGTPRYR DYADYIVRHE RAPGVGLLAG
     WRGDGSQHGK GAPNPAQLER YRENGGFWSA DVPAAGRYFK MANRDYLAWS QSMGFIARAE
     PVVLQLYSET LQKFRLAAQG HGPVLPPEAE RDRVATYFDP LPMWYEPFEG ARLEPGRFPL
     SAVTQRPPFM YHAWGSQNAW LRQIAARNYL YLHPETAARH GLADDDWVHV DSHHGRITVP
     CRLAGNVQPD TVWTWNAIGK RRGAWKLAAD APEATRGFLL NHLISDQLPG GDYANADPVT
     GQAAWFDLRV SLRKAGAGEE SHPQFAPLGD NPDTTPLRYG AGFRRAGP
//
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