ID A0A151BLZ2_9ARCH Unreviewed; 617 AA.
AC A0A151BLZ2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=AYL32_008890 {ECO:0000313|EMBL:KYH40916.1};
OS Candidatus Bathyarchaeota archaeon B26-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1779371 {ECO:0000313|EMBL:KYH40916.1, ECO:0000313|Proteomes:UP000075437};
RN [1] {ECO:0000313|EMBL:KYH40916.1, ECO:0000313|Proteomes:UP000075437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B26-2 {ECO:0000313|EMBL:KYH40916.1};
RA He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT phylum Bathyarchaeota widespread in marine sediments.";
RL Submitted (MAR-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:KYH40916.1}.
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DR EMBL; LUCE01000021; KYH40916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151BLZ2; -.
DR STRING; 1779371.AYL32_008890; -.
DR PATRIC; fig|1779371.3.peg.1908; -.
DR Proteomes; UP000075437; 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 8..210
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 617 AA; 67857 MW; 2309A336D773EE66 CRC64;
MTNGWRGYTG RILRVDLSEG TIRTEELDED DAFRFIGGSG LAAKIIYDEV DPSIDPFSPE
NRLVFMTGPL EGTIVPCSCR YVVAAKSPLT EAWGEAHASG FWGPELKAAG YDGVVVEGKA
SSPTYIKITD GDVELLDASG LWGLGCLDTE RALKADYGGR FRVVCIGPAG ERLVRYASII
GDGGRTAGRC GMGAVMGSKN LKAIIVKGSS RVQVADPKRL RSMIRRLYPV IMSFPTTQIH
SAYGTNGEMG PFYEYGDVPI KHFTIGVWEG ISKIDGDAMA ESIVKGQRAC PGCPIGCTRY
IKIESGPYAS VEGKGPEYET AASLGSLLLN DDIESIAKAN ELCNQYGLDT ISTGVSIAFA
MELYERGIIT KADTGGLELE WGEPATILRL IEMIGRREGF GDTLAEGVRR ASEIIGRGSR
RYAMHVKGLE MPMHDPRAFK GMGLQYATSN RGACHMQGFV LRIEQGERMV DLKIYERVDR
FETRGKGRIV AIMQDWHEIL DSMILCKFLS VSPGHVASLY TLVTGITLRL PEMLEAGERI
YNLKRLFNVR CGITRRDDAL PERFLKEPLP DGGAEGQTVN LEEMLKEYYE YRGWDENGAP
TIETLRRLGI TEKTHQS
//
