ID   G4RLE3_THETK            Unreviewed;       614 AA.
AC   G4RLE3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   02-SEP-2026, entry version 52.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase 3 {ECO:0000313|EMBL:CCC82388.1};
DE            EC=1.2.7.- {ECO:0000313|EMBL:CCC82388.1};
GN   Name=aor-3 {ECO:0000313|EMBL:CCC82388.1};
GN   OrderedLocusNames=TTX_1768 {ECO:0000313|EMBL:CCC82388.1};
OS   Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS   / Kra 1).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC82388.1, ECO:0000313|Proteomes:UP000002654};
RN   [1] {ECO:0000313|EMBL:CCC82388.1, ECO:0000313|Proteomes:UP000002654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC   {ECO:0000313|Proteomes:UP000002654};
RX   PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA   Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA   Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA   Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA   Hensel R.;
RT   "The complete genome sequence of Thermoproteus tenax: a physiologically
RT   versatile member of the Crenarchaeota.";
RL   PLoS ONE 6:E24222-E24222(2011).
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; FN869859; CCC82388.1; -; Genomic_DNA.
DR   RefSeq; WP_014127642.1; NC_016070.1.
DR   AlphaFoldDB; G4RLE3; -.
DR   STRING; 768679.TTX_1768; -.
DR   PaxDb; 768679-TTX_1768; -.
DR   GeneID; 11262652; -.
DR   KEGG; ttn:TTX_1768; -.
DR   PATRIC; fig|768679.9.peg.1789; -.
DR   eggNOG; arCOG00706; Archaea.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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   InterPro; IPR051919; W-dependent_AOR.
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:CCC82388.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002654}.
FT   DOMAIN          4..210
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   614 AA;  67874 MW;  7BAE7524A6B2A8F5 CRC64;
     MAIFRVARID LSTEKVTEEV YKDDVLKKFL GGRGLGSYLA LKEIPRGIDP FSPSNRLYIF
     AGPLSAMANL STSRVTVVTK SPLTGSLTHA NAGGNFAYWL RKSGYDGLII EGSSEEPVYV
     VVKDGDVAIK PARHLWGRWT GAAVKAILRE NGFPEEEKAA GVAVIGPAGE NLSRIAGIRM
     SDYERFAGRG GVGAVMGSKK LKGILVWGTR DLLKDVKDRA KFIAESTKLA QRLMSGPTAK
     ALHIYGTNLL TAVINSIGAY PTRNFETAYA EEADKLTGEY IKKNYVVETH ACMMCPIGCT
     QHVMVKGGPF KFIGKAKYEY ENTWSLGANI GLFDPEADLR LQKLANELGF DTISLGNTLA
     AALELAKMGK LPVNIDWGDA GALVDLVIRM ANRSDIGDDL AEGDYRLALK YGEPRVFRGS
     RGQGLPAYDP RSLKGFALSY FTANRGGDHL EAYSPTWEVL GVPEKVDPLC ETPECIEKQA
     RIVIYAQHLM ALTDSVTYCK FATLDREGIF EKDLAYLFNL AYDWDVTPED MLTIGERIFN
     VERLFHVKEG KWVKDELNPH FRNPIPTGPA KGHTAAKMFD EGIKIYYKLR GWVDGKPTYD
     TLKRLGLEEF QYLL
//