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Database: UniProt
Entry: A0A0F8AVN3_9EURY
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ID   A0A0F8AVN3_9EURY        Unreviewed;       643 AA.
AC   A0A0F8AVN3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   ORFNames=FK85_24920 {ECO:0000313|EMBL:KKF39911.1};
OS   Halorubrum saccharovorum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39911.1, ECO:0000313|Proteomes:UP000053331};
RN   [1] {ECO:0000313|EMBL:KKF39911.1, ECO:0000313|Proteomes:UP000053331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|EMBL:KKF39911.1,
RC   ECO:0000313|Proteomes:UP000053331};
RA   Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT   "Full genome sequence of Halorubrum H3 strain isolated from Burlinskoye
RT   Salt Lake (Altai Krai, Russia).";
RL   Submitted (MAR-2015) 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:KKF39911.1}.
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DR   EMBL; JNFH02000010; KKF39911.1; -; Genomic_DNA.
DR   RefSeq; WP_050023817.1; NZ_JNFH02000010.1.
DR   AlphaFoldDB; A0A0F8AVN3; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000053331; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053331}.
FT   DOMAIN          7..212
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
FT   REGION          620..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   643 AA;  69108 MW;  8D423F40E2FEE12F CRC64;
     MTEMGGYRDR VAQVDLGDGA VDYRGIDEDD AEKYIGARGL GVKYVFDAGP DVDPLGPDNR
     LAIMTGPLTG TQTVMSGRIA FVTKSPLTGT VTDSHHGGWS GARLKWSGLD GLLLDGASDE
     PVYLFVEDGE VEVRDASHLW GEGVHDTIDA IGEEVDGKVG RNVSVMAIGQ GGENEVRYGC
     VINEDDRASG RGGTGAVMGS KNVKAVVVKS GTNMPKPADP ETFQEGYQQA MEVIRESDVT
     APNEGGLSMY GTNVLMNATE EMDGLPSKNA KYTSTEAYNE AEGVDIEAER VSGENVRENI
     LVDEPTCHSC PVACKKEVEV DVTHKGQDMN VRTESYEYES AWALGPNSGH SDRDEIALML
     QRCNDLGIDT IEAGNMMAMA MEMSEEGKLD GVGHLDWGDS ETMIDLLDEI GHRSSDLGDL
     LAEGPERVAD AKDAHGNKLS VKGQTMAAYD PRCMKGMGIA YATSNRGACH LRGYTPAAEI
     LGIPEKVDPY EWEGKGELTA TFQDLHAVSD SFDICKFSAF AEGIEEYVLQ YNGVTGRDVS
     EDELFEAGER VYNLERYYNN LVGFDGADDT LPNRFIDGHP DAIPGTGASE GQLAELDEMK
     AEYYETRGWV DGVVPDEKLD ELGIDIGPGT GVSTGDSAAP ADD
//
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