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Database: UniProt
Entry: M1NFY9_DESSD
LinkDB: M1NFY9_DESSD
Original site: M1NFY9_DESSD 
ID   M1NFY9_DESSD            Unreviewed;       420 AA.
AC   M1NFY9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Putative adenylylsulfate reductase-associated electron transfer protein QmoA {ECO:0000313|EMBL:AGF78574.1};
GN   OrderedLocusNames=UWK_02025 {ECO:0000313|EMBL:AGF78574.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78574.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the HdrA family.
CC       {ECO:0000256|ARBA:ARBA00006561}.
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DR   EMBL; CP003985; AGF78574.1; -; Genomic_DNA.
DR   RefSeq; WP_015404265.1; NC_020304.1.
DR   AlphaFoldDB; M1NFY9; -.
DR   STRING; 1167006.UWK_02025; -.
DR   KEGG; dsf:UWK_02025; -.
DR   PATRIC; fig|1167006.5.peg.2215; -.
DR   eggNOG; COG1148; Bacteria.
DR   HOGENOM; CLU_020302_1_0_7; -.
DR   OrthoDB; 9766627at2; -.
DR   Proteomes; UP000011721; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR039650; HdrA-like.
DR   PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR   PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
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:UP000011721}.
FT   DOMAIN          101..129
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   420 AA;  45299 MW;  C44310BEDE08984B CRC64;
     MTDEQGTSGA ILVVGGGISG LTAALEAAEV GNDVYLVEKN AYFGGRVAQL NQYFPKLCPP
     SCGLEINFKR IKDNRRIRTY TMTSVTAVSG GPGNYEVTLE TSPRYVNSNC TACGECADAC
     PDEIDNEFNF GMNKSKAAYL PHEMAFPRRY VINKEALTSA GADAVKASCK YGAVDLDMAT
     ESKTINVASI IWATGWTPYD PTKMDNLKFN ESNAIVTNMM IERMAAPGGP TNGAILRPGD
     NKEPESFAFV QCAGSRDENH LEFCSYICCM ATFKQMTYIR ERYPEAKIYV FYIDLRTPGK
     YEKFREKLMK DANSTFIKGK VAEIIPESDG SVTVVAENAV TGEKIKQNVD MAVLATGMQP
     SLAVNGTPVA LDTDPSGFVN SNPETGVLSA GCACRAADVV TSNQSATAAA LKAIQVSRRS
//
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