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
//