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Database: UniProt/TrEMBL
Entry: I4C504_DESTA
LinkDB: I4C504_DESTA
Original site: I4C504_DESTA 
ID   I4C504_DESTA            Unreviewed;       701 AA.
AC   I4C504;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:AFM24645.1};
GN   OrderedLocusNames=Desti_1938 {ECO:0000313|EMBL:AFM24645.1};
OS   Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC   Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC   Desulfomonilaceae; Desulfomonile.
OX   NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM24645.1, ECO:0000313|Proteomes:UP000006055};
RN   [1] {ECO:0000313|Proteomes:UP000006055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC   {ECO:0000313|Proteomes:UP000006055};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL   Submitted (JUN-2012) 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; CP003360; AFM24645.1; -; Genomic_DNA.
DR   RefSeq; WP_014809790.1; NC_018025.1.
DR   AlphaFoldDB; I4C504; -.
DR   STRING; 706587.Desti_1938; -.
DR   KEGG; dti:Desti_1938; -.
DR   PATRIC; fig|706587.4.peg.2228; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_0_0_7; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000006055; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000006055}.
FT   DOMAIN          7..209
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   701 AA;  77938 MW;  1699029CD9E01832 CRC64;
     MAKYGGWAGK VLRVDLSGRK ISTEDTVEKY KDYLGGTGIG YKVIWDELHA GIKPFDPDNK
     IVFGVGPLAG TGAPCNGRTA ITTLWPTCWP RPLVASGHMG GHFAAELKYA GYDAIIIEGR
     ADRPVWLSIM DGKAEIKDAR QLWGQGIRRT TVEISHEMGP EASVAAIGQA GENLVPMSVV
     INSYSHSAGG VGGVLGSKNL KAIGVRGTGS VRIAGNKVEW EKVIKLHLSL LGANNQHVVP
     NSPQPWSEHY NPGSRWVASA GRRWGAAYPG IETGPCEPHN LNRIAYRTNN AAFFLGEKAW
     KYTIRGNGCT ACPIRCHTML KVPGVSTKYG ILETGQNTCV GLLFGKAFFK NFPDGPKGET
     AIEACMVGMH LADDLGLWEN YGQLQRDFQM LYYNGTMSRK VPEKEFKGYS WDKYEQGDPT
     FLFELLPRIA RKEGELATAL GLGTGYLLER WGIPEQEWLE NRDLLYWKLG HPKHHSNEDA
     GQCGVIINTQ YNRDAQCHSH SNFTRNGLPI EVQKRLAAEI WGSPDAVDSV AAFAPMNKYK
     AKMAKWSLLR KELHDSLSLC NWMGPWVASP LRERDYRGDD SIESLLYSLA TGDKKTSQEL
     DRVAERIFLL HRALTIRDMG TKDMRTKHDT IPHWVFTDPK DKAAFSKGTI RMDEEDIKLA
     MDMYYEEMGW DKQTGSPTGD TYQRLGLGFV AEYLSKKGLL P
//
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