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Database: UniProt/TrEMBL
Entry: A0A1J1AEB1_9EURY
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Original site: A0A1J1AEB1_9EURY 
ID   A0A1J1AEB1_9EURY        Unreviewed;       589 AA.
AC   A0A1J1AEB1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   Name=aor {ECO:0000313|EMBL:APE96253.1};
GN   ORFNames=HSR6_1817 {ECO:0000313|EMBL:APE96253.1};
OS   Halodesulfurarchaeum formicicum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halodesulfurarchaeum.
OX   NCBI_TaxID=1873524 {ECO:0000313|EMBL:APE96253.1, ECO:0000313|Proteomes:UP000186165};
RN   [1] {ECO:0000313|Proteomes:UP000186165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSR6 {ECO:0000313|Proteomes:UP000186165};
RA   Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA   Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Smedile F.,
RA   Messina E., La Cono V., Yakimov M.M.;
RT   "Discovery of first anaerobic lithoheterotrophic haloarchae widely
RT   represented in hypersaline habitats.";
RL   Submitted (AUG-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}.
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DR   EMBL; CP016804; APE96253.1; -; Genomic_DNA.
DR   RefSeq; WP_071933422.1; NZ_CP016804.1.
DR   AlphaFoldDB; A0A1J1AEB1; -.
DR   GeneID; 30418349; -.
DR   KEGG; hhsr:HSR6_1817; -.
DR   Proteomes; UP000186165; 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   ECO:0000313|EMBL:APE96253.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186165}.
FT   DOMAIN          13..207
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
FT   REGION          525..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  62933 MW;  807E8D2A3A8C9D40 CRC64;
     MTTERAPPRR TAVLRVDLTD GTVKREPIPE QWLRQYIGGK GLGARYLHEV TEPGVDPLAP
     GNALLFMVGP LSGLIPGEPR YAAITKSPLT GTFLDSYSGG DFAARLAGSL GETMGLIVTG
     QAPEPVSLVV SDGDVSIEPA TAWGEGVEAA CEAHPDAAVA CTGPAGENEV VYATIASDGG
     DHHAGRGGAG AVMGSKRLKA VIAVDEPVSG LDELRTEYEE RFGDGSTDDW HRASETVESV
     DFADEIGALS TRGWQESTFE GTDEIGIEAV EATDYEREHE GEAIPGGFRV SFEESESTPR
     GGTQMTLGAG LGIDDFEDVA TLGLTCDRLG VDIIGVGNAI AWAIRAGEEG VIDYAGEFGD
     IESAIELAEA IAARETELGA TLADGIDAAA EAYGGEDLIP TVKGMELPSY DPRRAPSMAL
     AYATSDRGAC HRRARPIETA VFEPDLDEPT RRAREVIAEQ DYRSLLWSLI ADDFTETLYT
     RDFGAEWLAA VGLELTPTAL RRAGTRIWTL TRLFNVREGF DRDDDTLPPV LEEPITDGPG
     AGDQISQSEF EAMRSAYYEQ RGWDERGVPT RETLDALDLG ALFPSVNRA
//
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