ID S5ZN87_9CREN Unreviewed; 625 AA.
AC S5ZN87;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=N186_08490 {ECO:0000313|EMBL:AGT36036.1};
OS Thermofilum adornatum.
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=1365176 {ECO:0000313|EMBL:AGT36036.1, ECO:0000313|Proteomes:UP000015543};
RN [1] {ECO:0000313|EMBL:AGT36036.1, ECO:0000313|Proteomes:UP000015543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1910b {ECO:0000313|Proteomes:UP000015543};
RX PubMed=24029764;
RA Dominova I.N., Kublanov I.V., Podosokorskaya O.A., Derbikova K.S.,
RA Patrushev M.V., Toshchakov S.V.;
RT "Complete Genomic Sequence of 'Thermofilum adornatus' Strain 1910bT, a
RT Hyperthermophilic Anaerobic Organotrophic Crenarchaeon.";
RL Genome Announc. 1:e00726-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a
CC carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:16421, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001714};
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; CP006646; AGT36036.1; -; Genomic_DNA.
DR RefSeq; WP_020963343.1; NC_022093.1.
DR AlphaFoldDB; S5ZN87; -.
DR GeneID; 25406209; -.
DR KEGG; thb:N186_08490; -.
DR PATRIC; fig|1365176.7.peg.1679; -.
DR eggNOG; arCOG00709; Archaea.
DR HOGENOM; CLU_020364_1_0_2; -.
DR Proteomes; UP000015543; 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 Reference proteome {ECO:0000313|Proteomes:UP000015543}.
FT DOMAIN 6..223
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 625 AA; 69446 MW; 65B41B3ACEEB5956 CRC64;
MNIPGYNGKI LEVDLSRDKD RVIELDEETA YKFIGGRGLA AYILWKELGH KWEQVDPLGP
ENLLLFLTGP LTGYYPGVKL AVSGKSPQTN GVVGSVVSSE LAIELRAAGY DGLIVKGASK
DPVYIYIEGE KVEVRSAEHL WGLRGRETFQ KLFSEVWGEL KRKNLAHVGL TKEPSFVYIG
PAGENMVRTA AVMAKLTHAA GYGGYGAVMG SKKLKAVVAK GFGPMPPAKH PEWVKLLVRE
AWNRLNQNIF WKQWGTSSGG YEVANLTSSE PIRNWQEEWH DARTMGVNNY EAHWVKRYWG
DYGCPSTCMK ISRLIGGKYN GTVTDGPDYE LQAYLGPNLG VFEPRGNIYL SSLADDLGLC
GIQTGNVAGF AAELCEKGIL TREEVGFDLK WGDTEAFARL LEAIAYRKGI GDILAEGVAR
AADKLSKLKG QDLSRYAVHV KGIGIGAHGA RSGKDFPQAF TYAVGVQGGD HTSPPRLPVE
KAWGEFTAAF EDSAVICSFN AVDDLPYQFL TAITGWEISS EKWFREHARR IVSLQRVLLL
LGGPDLYWDP RIHDDNPPRF YEPLPSGPFK GKAVDRTELE KQKKEYFDYL GWDQYGIPRD
ETLKELGISE LSEATRRIRN RLKLE
//
