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Database: UniProt
Entry: M1NJE1_DESSD
LinkDB: M1NJE1_DESSD
Original site: M1NJE1_DESSD 
ID   M1NJE1_DESSD            Unreviewed;       942 AA.
AC   M1NJE1;
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=4Fe-4S protein {ECO:0000313|EMBL:AGF79684.1};
GN   OrderedLocusNames=UWK_03157 {ECO:0000313|EMBL:AGF79684.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF79684.1, 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; AGF79684.1; -; Genomic_DNA.
DR   RefSeq; WP_015405368.1; NC_020304.1.
DR   AlphaFoldDB; M1NJE1; -.
DR   SMR; M1NJE1; -.
DR   STRING; 1167006.UWK_03157; -.
DR   KEGG; dsf:UWK_03157; -.
DR   PATRIC; fig|1167006.5.peg.3402; -.
DR   eggNOG; COG1148; Bacteria.
DR   HOGENOM; CLU_004231_2_0_7; -.
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   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.30.70.3270; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR003953; FAD-binding_2.
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; PF00890; FAD_binding_2; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 3.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT   DOMAIN          24..54
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          71..105
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          857..886
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          890..919
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   942 AA;  102402 MW;  4A1BCD174BC9CCB7 CRC64;
     MITNADFLAL EGKPGNFTAK LNIRPRYIDA DACTACGLCT QYCPKHHADA YNEGLSITRP
     IHIDYAQAVP ATYYIDPASC MHIQYDTCQI CVPVCQSHAI NFSQKPESRD LKIGAVILSP
     GFGKIADETL EKFSYGKHPD VVTAYEYERM TTASGPFLGE IKCFSDGRHP KSMAFIQCVG
     SRDLGCDNGY CSSVCCMYAI KEALVTKEHD PEVDITIYYM DIRTQGKDFD AARERAEAIG
     IKFVRAKVAD VTPWENHLRL TYSTLDGQHK FDAHDMVVLS VGLESPKDAQ KISDITKIEL
     NKYDFCKTNS FTPLQTSQDG IVVAGAFQGP KDIPESATQS SGAAALAASI LKKQRGKGTI
     IKEYPSELSV TDEDEVRIGV FVCHCGINIS SVVDCPDVAD NAGTMDNVAY YTENLYSCSQ
     DAQEQIKKTI KDQKLNRVVI AACSPRTHEP LFQETLKDAG LNRNLFEMVN IRDQCSWVHA
     NEPEAATQKS KDLVRMAVSK AAHIQPLPEQ TVPVTPKALV IGGGIAGMTA ALSLADQGFE
     SILVEKSPSI GGNLKNLKNT LAGDTVGTFL KTLTAKVQKS AKITVITDGS LAQTSGFIGN
     FNSVIESGKG KNKKETVYDH GVIVVATGGH EHRPDLYELG KSKKVVTQQE LEAKLAGRTK
     NRAPNSIVMI QCAGSRGEDL NYCSKVCCNH AMKNILKIKE INPDSQIIVL YRDIRTYGFA
     EDAYLEARKK GVVFIPYETD RRPVVSSKGT KVQVDFFDSI MQEEVSMNPD LVTLSVGIVP
     DGTDELSKML KLPVNANGFF LEAHVKLRPV EAAVDGIYIC GLAHAPKPVE ETIVQAQAAA
     AKAAMPLVKG FVTVDPIVSS VEQDNCIGCG LCSSLCPYGA IIMEKVGKKR KARTISASCK
     ACGICASHCP TFAISMGGFT NEQLISQIEA FGNKITDEKV EA
//
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