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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//