ID   A0A117S2R0_9FIRM        Unreviewed;       611 AA.
AC   A0A117S2R0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN   ORFNames=APF76_18135 {ECO:0000313|EMBL:KUO48800.1};
OS   Desulfitibacter sp. BRH_c19.
OC   Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC   Desulfitibacter.
OX   NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO48800.1, ECO:0000313|Proteomes:UP000053015};
RN   [1] {ECO:0000313|EMBL:KUO48800.1, ECO:0000313|Proteomes:UP000053015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO48800.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUO48800.1}.
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DR   EMBL; LOER01000047; KUO48800.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117S2R0; -.
DR   STRING; 1734395.APF76_18135; -.
DR   Proteomes; UP000053015; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
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          6..207
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   611 AA;  66703 MW;  379D75C7688EED1A CRC64;
     MIKPGYSGKI LTIDLTKRSF MVNDLPEDLI EKYLGAKGFG AKILYDELPP NCDPLSPENI
     IMFATGPLTG TLVPASSRSV IVTKSPLTGI WLDSNCGGTF GPELKSAGFD IVKIIGKADK
     PVYVLIKDNE ILIKESEELW GTDALTTHIC LKKKYGEDYK IACIGEAGEK QVLVASVIAE
     GRAFGRGGPG AVLGSKNLKA LVVSGSNAIN IHNYHEFMIA NREAKNEIAI SPDTGGSRPK
     FGTSSIYSFI REGGALPVKN FQGGTYPGAE EVDEHLLVKE LYDKDRSCFA CPIACSKHST
     VKKGKYSGKF VEGPEYENVW SFGAQCGNSD IGAVVYAEYL CDYYGIDSIS VGNTIGFAME
     CFEKGLVTKE QLGFECRFGN DEAIIKLIHL IGKREGFGEV FGQGVRKASK EIGSDSKHFA
     MHVKGLELPA YDPRAAFGMG LAYATSDRGG CHLSAFPVKT ELLSSNHRID PLSIEFKAEL
     VKNEQDWFSV IDSLGICLFA IFALGPNQIT DLLYCLTGQK SFSSAEQLIN IGERINNLTR
     LFNLREGLTA TDDTLPPRLL KDTLQEGPSK GQTVPLEEML KEYYLIRGWN QEGRPTAKKL
     QQLELTNDVN G
//