ID   B8J1R4_DESDA            Unreviewed;       579 AA.
AC   B8J1R4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ACL49672.1};
DE            EC=1.2.7.5 {ECO:0000313|EMBL:ACL49672.1};
GN   OrderedLocusNames=Ddes_1775 {ECO:0000313|EMBL:ACL49672.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49672.1};
RN   [1] {ECO:0000313|EMBL:ACL49672.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49672.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) 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 AOR/FOR family.
CC       {ECO:0000256|ARBA:ARBA00011032}.
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DR   EMBL; CP001358; ACL49672.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8J1R4; -.
DR   STRING; 525146.Ddes_1775; -.
DR   KEGG; dds:Ddes_1775; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_7; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR   Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR   Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR   InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR   InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR   InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR   InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR   InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR   InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR   PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR30038:SF0; TUNGSTEN-CONTAINING ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR   Pfam; PF01314; AFOR_C; 1.
DR   Pfam; PF02730; AFOR_N; 1.
DR   SMART; SM00790; AFOR_N; 1.
DR   SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR   SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 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   ECO:0000313|EMBL:ACL49672.1}.
FT   DOMAIN          1..208
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   579 AA;  61591 MW;  A77B7CA5B16809F3 CRC64;
     MFRFLRVNMA TRTCVFEEIP QEYAGLGGRA LTSTIVAREV PPTCTAIGPH NKLVFAPGLL
     GATNSPNANR ISVGCKSPLT EGIKESNAGG QPGGHLARLG ILAVIVENMA EEGQWWQLEI
     GKDHARLVPS DVAGLNNFDA VAKLVEKHGE TCSYISIGRA GEFKLTAASI ACTDRELRPM
     RHAGRGGVGA VMGSKGLKAI IINPEGGKNQ PLQDEKAFRE ASKRFAKALA EHPITSKGLA
     DYGTAVLVNI LHEAGGLPTA NFTVGRFDQH ESVSGELLNQ MTKERGGTVA HGCMSGCMIR
     CSGILPDKKG KFQSKWPEYE TLWAFGPHSG IGDMDAISKY DYMCDDIGVD TIDVGVAMGV
     AMAGGAIPYG DAMAVMDAMH AISEGTPLGR IIGCGTATTG RVFGVRRVPT VKGQSLPAYD
     PRAVKGQGVT YATSPMGADH TAGYAVTANI LSSGGTVDPL KKEGQIELSR NLQVATASVD
     SVGLCLFTAF AILDVPDALP AIVDMLNAKF GWQLTGDDVV TLGQRILSTE IDFNRRAGIT
     QAADVLPDFF TDEKFPPHDT TFDITHDELK TVFNWIEEK
//