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Database: UniProt
Entry: A0A151FAY8_9EURY
LinkDB: A0A151FAY8_9EURY
Original site: A0A151FAY8_9EURY 
ID   A0A151FAY8_9EURY        Unreviewed;       595 AA.
AC   A0A151FAY8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   ORFNames=AYK18_08425 {ECO:0000313|EMBL:KYK38032.1};
OS   Theionarchaea archaeon DG-70.
OC   Archaea; Euryarchaeota; Theionarchaea.
OX   NCBI_TaxID=1803813 {ECO:0000313|EMBL:KYK38032.1, ECO:0000313|Proteomes:UP000075311};
RN   [1] {ECO:0000313|Proteomes:UP000075311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYK38032.1}.
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DR   EMBL; LSSB01000042; KYK38032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151FAY8; -.
DR   Proteomes; UP000075311; Unassembled WGS sequence.
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}.
FT   DOMAIN          4..208
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   595 AA;  66155 MW;  9EDF7A993488688D CRC64;
     MYSYTGKILR IDLSRDKISE ESLNEKDARK FIGGKGLGAK LLFDNMDPRT DPLSPDNPLI
     LCTGPLTGSS APTSGRWCVV TKSPLTSLYL DSHVGGYFGA EMKKSGHDII IIKGKANSPV
     YISINDNDVQ IKEANHLWGK NTTATEEALK EEGRVLSIGV AGEKMVRFAC INTDLFVHNG
     RGGNVGRGGA GAVMGSKNVK AVVIKGSHKM EYSDEQKFRD AVKKALTMIN ENSFIPTRRK
     YGTPIWVNPV NENQLLPTYN FSRGSFEKAD NISGETMHDT IVVKNKSCFN CPIACGKWTR
     FEFNGKQYEF EGPEYESIAL LGSNCGNETI QGTAYVSYLC DEYGLDTISA GNVVGFAIEA
     VKKNLIDEKV DFNDPKTQGE LIRKIAYREG IGSDLAEGVK RFSEKYGGTE YAIQSKGMEF
     PGYDPRGAFG MALAYATSDR GACHQRVWTV RAEMQGDLAP RYGIEGRAEF VKENQDERAC
     CYSLVLCDFA PLSVDMFVEL LNTATGFQYS AEEYLKTGER IWNLTKMFNV KNGVTRKDET
     IPKRILEEPL EKDEAYIGRE NFEQMLSEYY TLRGWDENGV PTTETLKELN LEGFA
//
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