ID   C6BXM6_MARSD            Unreviewed;       647 AA.
AC   C6BXM6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ACS78584.1};
DE            EC=1.2.7.5 {ECO:0000313|EMBL:ACS78584.1};
GN   OrderedLocusNames=Desal_0517 {ECO:0000313|EMBL:ACS78584.1};
OS   Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS   VKM B-1763) (Desulfovibrio salexigens).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Maridesulfovibrio.
OX   NCBI_TaxID=526222 {ECO:0000313|EMBL:ACS78584.1, ECO:0000313|Proteomes:UP000002601};
RN   [1] {ECO:0000313|EMBL:ACS78584.1, ECO:0000313|Proteomes:UP000002601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763
RC   {ECO:0000313|Proteomes:UP000002601};
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., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL   Submitted (JUN-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; CP001649; ACS78584.1; -; Genomic_DNA.
DR   RefSeq; WP_015850403.1; NC_012881.1.
DR   AlphaFoldDB; C6BXM6; -.
DR   STRING; 526222.Desal_0517; -.
DR   KEGG; dsa:Desal_0517; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_7; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000002601; Chromosome.
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:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE: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:ACS78584.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002601}.
FT   DOMAIN          4..205
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
FT   REGION          558..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   647 AA;  71226 MW;  9B57B1DA3AED15AC CRC64;
     MHGWAGWILR VDLGSGAINK IPLNPDIAQK FIGGRGLNSL TLFNEVGPHI DPLSPENVYC
     FGAGPLSGTP LGLTSRVEVS TLSSYSGILG DGNAGGSLAF MMKRAGLDQI IISGQAEAPC
     YLLVEDGRAK LHSAEELWGL SVWETTDKLQ EKHGKSSSVA CIGQAGENLV RVATTMVDKY
     ASAARGSGAV LGSKKLKAVV VKGSGRISLA DADKFKELAA EDRNFFKESD FQRDIVGQYG
     THIGMLMWEP GFRNYEKYWR GADVPDNLRP EAWKEFSIGR HGCHGCHVRC KDYYRIPSGS
     RAGESGKAME YECIFCLGTN CGITDPVAIM EMENICDAYG MDVLALGNTV AMLKDLYSRG
     MVSKELSDGL DLSWENHTDQ IELLHRTAMR QGLGNLVAEG MYTLAKRLGG QAMDYCYHVK
     GLSRGPYPSG VFSLAHATST RGADHLRGRS WAFSQPDPDM FPILKEQGLL MENVDDDPAP
     AVIVGERMTT LTDCIGRCKG AVNNWISAMP LVWKKPIFEG LAELLSAATG EDYTAEKLEQ
     AADRVYALEH AFNIRQGTTR RDDRMPQKPE IRDTEEGKAD LRKHEQHLSR YYELRGYDQH
     GCPTPERLKE LELEFVCQGL ADTPARKEWD GPPMCELEDY PCGGKRC
//