ID A0A256Z888_9CREN Unreviewed; 613 AA.
AC A0A256Z888;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=B6U85_01215 {ECO:0000313|EMBL:OYT48835.1};
OS Desulfurococcales archaeon ex4484_42.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales.
OX NCBI_TaxID=2012520 {ECO:0000313|EMBL:OYT48835.1, ECO:0000313|Proteomes:UP000216823};
RN [1] {ECO:0000313|Proteomes:UP000216823}
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:OYT48835.1}.
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DR EMBL; NJDT01000005; OYT48835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256Z888; -.
DR Proteomes; UP000216823; 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:SF5; 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 613 AA; 68111 MW; C10583AB839B3265 CRC64;
MKGWNGKGLL IDLSERKFKY FDIDATILKE YIGGRGLAIR LLWDLNPVGV DPLSPDNHLI
FAVGPLTGYP LPSSGKLVVA SKSPLTGGYG DGNIGVKAAV EMRKAGIDVL ILKGKADKPT
LIHVTSKGVE LINADDLWGL TTYDAEDRIR KVYGKNVGVL LIGPAGENLV RYATVVAEYG
RSGGRPGMGA VMGSKNVKAI VIEGDKLPEP HDPAKLRELG AEAYRKVKES PNYGFWMRQG
TMATIEWSQK ASVLPTYNFS EGVFDYADKI SGHVMESKRV LQKGCPLCNM PCGHTVKYGV
SEEGIEGKAE LDYENVAMLG SNLGIGDLDK VSHLNRLADE YGIDTISLGN VLGFTMEATE
KGIIRDEGIK WGDFKGAIEL TRKIVFREGI GEILSLGVRE ASKRLGRDSH KFAMQVKGLE
ISAYDCHAAP AMALAYGTSP IGAHHKDAWI IAYEVQTDRF AYSEEKVRRL VWLQNVRGGV
FESLVTCRLP WVEVGLDLDF YPKLLQAATG VTYTWDDLEL VANRIYTLIR MFWIREYKAT
GIEWGKHLDY PPDKWFERPL TKGPLAGAKL NREKYDSMLM KYYELRGWDK RGVPKRETLE
KLDLGFTLKY ITP
//
