ID A0A256ZUK6_9ARCH Unreviewed; 590 AA.
AC A0A256ZUK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=B6U77_00115 {ECO:0000313|EMBL:OYT56292.1};
OS Candidatus Hecatellales archaeon ex4484_218.
OC Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia;
OC Candidatus Hecatellales.
OX NCBI_TaxID=2012511 {ECO:0000313|EMBL:OYT56292.1, ECO:0000313|Proteomes:UP000215840};
RN [1] {ECO:0000313|Proteomes:UP000215840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (JUN-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:OYT56292.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NJEB01000002; OYT56292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256ZUK6; -.
DR Proteomes; UP000215840; 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..206
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 590 AA; 64984 MW; 8923595E0067EE97 CRC64;
MYGWNGKILV VDLSNKTLKT LTINENVLSE YMGGRGFGVK FLWELTNPTI DAYSADNVLV
FAVGPLTSTL IPTTGRFTVT AKSPLTGGIF YSSCGGFFGF KLKNSGLDAL VIKGRCEKPV
YLQIDDETFQ LKDATHLWGK TTKETIKILE EDLGKDYSFA CIGPAGENLV RFACIRGGDG
NFAGRGGLGA VMGSKKLKAI AVKGTRKTKI ADEKSLTELM KKIRVRISWN PVLSKALAYY
GTSALVNIIN EHEILPTKNF QLSRFKDAEK ISGEALREKI FVGRKSCYNC PVACKRVVKL
ENMKVEGPEF ETLGSFGSML MVNSLEAIVE INQLCNELGL DTISTGGTIA CAMELSEKNV
LDEKIGWGDV EKIKKLIVDI AYRKGLGDKL AEGSKIFSER IGFSDVSMQV KGLELPMYHP
DGVLGQALAY TTSNRGGCHL NAYLISVEIL GYPYLMDRFS PVNKPNIVAY LQNLAAVMDS
MVICKFLGFE FDEETFAKLL VAVTGKPYTQ ESVVAAGERI WNLERVFNFK AGLKGEEDKL
PSRFKVDVKP MLKEYYEVRG WKPDGFPSKN KLKNLGLKVE EDAVGSQGSL
//
