ID A0A1S6IY23_9FIRM Unreviewed; 576 AA.
AC A0A1S6IY23;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:AQS59684.1};
GN ORFNames=B0537_11705 {ECO:0000313|EMBL:AQS59684.1};
OS Desulforamulus ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS59684.1, ECO:0000313|Proteomes:UP000189464};
RN [1] {ECO:0000313|EMBL:AQS59684.1, ECO:0000313|Proteomes:UP000189464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSS09 {ECO:0000313|EMBL:AQS59684.1,
RC ECO:0000313|Proteomes:UP000189464};
RX PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT compost.";
RL Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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}.
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DR EMBL; CP019698; AQS59684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6IY23; -.
DR STRING; 1833852.B0537_11705; -.
DR KEGG; dfg:B0537_11705; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000189464; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189464}.
FT DOMAIN 1..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 576 AA; 60586 MW; D915AFECA4E51291 CRC64;
MPKFLRIDMT NLQLKWEECP EKYLALGGRA LTSQFVLDEV PATCHPLGEY NKLIIAPGLL
SGTNAPSSGR LSVGAKSPLT GGIKESNAGG ICSQKIANLD IKAIVVEGQP KEKGFWMVKI
SPEGAEILPA NDLAGKGTYE VTDILRQRYG SKVGVITIGP AGEMLLAGAG VTNNDSDGNS
SRYAGRGGLG AVMGSKGLKA IVVDAPKTFD VPVKDKERFS AAAKKFAKIL TSHPVCGEGL
PAFGTNVLMN IINEAGTLPV RNFSNNGRFD LANNVGGETL AEVAKARGGK ATHACHPGCV
MRCSNVYPMP DGKVCSPIEY ETAWCFGPNL EISDLDVVAK LNYLCNDIGL DTIEMGVALG
VLMEAGVIPF GDAEAAIKAL EEVGQGTPAG RILGNGAVFV GKAYGVTRVP AVKGQGIPAY
DPRSCKGNGV TYATTPMGGD HTAGYAVTAN ILKVGGFVDP TKAEGQVDLS RNLQIATAAV
DSTGLCLFVA FAVLDNPEGL PTVVEMLNAQ YGLNLTVDDV TKLGQSVLKN EREFNAKAGF
TSADDRLPEF FYSEKLAPHN TVFDISDEEL DSVFNF
//
