ID A0A2H9I0M7_9ARCH Unreviewed; 618 AA.
AC A0A2H9I0M7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=CP083_03290 {ECO:0000313|EMBL:PDM26560.1};
OS Candidatus Bathyarchaeota archaeon B24-2.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=2041147 {ECO:0000313|EMBL:PDM26560.1, ECO:0000313|Proteomes:UP000228824};
RN [1] {ECO:0000313|EMBL:PDM26560.1, ECO:0000313|Proteomes:UP000228824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B24-2 {ECO:0000313|EMBL:PDM26560.1};
RA Feng X., Perumal V., Wang F.;
RT "Metabolic analysis of an uncultured genome Bathyarchaeota B242 based on
RT metagenomic technology.";
RL Submitted (SEP-2017) 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:PDM26560.1}.
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DR EMBL; PCNA01000022; PDM26560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H9I0M7; -.
DR Proteomes; UP000228824; 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 618 AA; 67682 MW; 930E9EE043107DF0 CRC64;
MFGYAGRILH VNLTTGKIST EPLKEDLAKN YIGGIGLGIR LLLDHSTPGV DPFSPDNPLI
LTAGPLGGTM APTAGNGHAF VSKSPASLGV GESKSHGFFA ADLKRAGYDA VIFKGKAEKP
VYLWIDDDTV ELLDAQHLWG KSPAETEDII KEELGDYYIR VAAIGPAGER LMRLACILND
KTRAAGRTGL GAVMGSKNLK AIAVRGTRDI RVAKPDEFLE FVRELHEREK GPATRKYRTL
GTPQNVLVHN ALGALPTRNF TNATFEGAER VSGEYLNQRF VVKIIGCSSC AQRCEHIAVV
PEGPYKGTTV RVEYETLWAF GPNCGVDRLD AVIKAIDICN YYGMDALGTG VVISFAMDCY
EHGILTKEDT GGLELNFGNH EAMLELLRMI GERKGLGDIL AEGSKRAAEK IGKGAEKYAC
HIKGVELTGY DLRSLKTAAL GFAVSFRGAD HNRHGAYSPD LSGKVDRFKA DKSKGKVVKD
IEDLYTIIDS LIVCKFSRGI YYEGFADLAK LYTLVTGIEM SAEDMRRAGE RINNIARLFN
VREGFSRKDD TLPYKIMHFP VPDEGVVSHG SYVSQKELDI LLDGYYEVRG WTKEGIPTLE
KLNELGLNDL AYIVKDKL
//
