ID A0A0P6XXZ8_9CHLR Unreviewed; 722 AA.
AC A0A0P6XXZ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 02-APR-2025, entry version 26.
DE SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:KPL85072.1};
GN ORFNames=ADN01_06775 {ECO:0000313|EMBL:KPL85072.1};
OS Levilinea saccharolytica.
OC Bacteria; Bacillati; Chloroflexota; Anaerolineae; Anaerolineales;
OC Anaerolineaceae; Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL85072.1, ECO:0000313|Proteomes:UP000050501};
RN [1] {ECO:0000313|EMBL:KPL85072.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL85072.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-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 -!- COFACTOR:
CC Name=tungstopterin; Xref=ChEBI:CHEBI:30402;
CC Evidence={ECO:0000256|ARBA:ARBA00049934};
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:KPL85072.1}.
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; LGCM01000027; KPL85072.1; -; Genomic_DNA.
DR RefSeq; WP_062418552.1; NZ_DF967974.1.
DR AlphaFoldDB; A0A0P6XXZ8; -.
DR STRING; 229921.ADN01_06775; -.
DR PATRIC; fig|229921.5.peg.2242; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000050501; 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 InterPro; IPR051919; W-dependent_AOR.
DR PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR PANTHER; PTHR30038:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE: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:UP000050501}.
FT DOMAIN 30..248
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 722 AA; 80964 MW; 6713CECEBB74EB4A CRC64;
MTVLSPAAAR EAHQLLAEFS YDLRPVERGY ANRTLYVNLG DLTIQSKPVT EEMKRVFTGG
RGFGLWLLWN GTRPETRWND PENELVITGG VIGGISNYPG SGKCTAVTIS PQTGVPIDSN
SGGYFGPYLK FAGWDAIEIQ GKAEQDVIII VDGDLGEVRV ETAPLEPVDT HLIARLLTDM
YGDTPKEKRG ISVVSAGQAA DHVAMCGLNV SYYDPRRDEI RYKQAARGGA GRVLRDKHIK
AIVVRYSNMN ANSNGVADMA LLQKAGQRIN REITQFDESQ NDMRGTGTPY LVEIMNRFDL
LPTQNYRFGA HDEAHKIAGD VWKPQFDRRG PDGCWYGCTM ACAHAVNEYE LRSGPYKGQK
VFVDGPEYET LGGLGSNLNI FCPNDILELN FYCDTYGIDT ISAGNSIAFV MECWENGILT
KEHTGGLDFT WGNTDAALEL LHQMARGEGF GLIVGQGIRH MKAYFVEHFG ADAAFLQDIG
MEVKGLEISE YMTKESLTQQ GGYALASKGA QHDEAWLIFM ELVHKQLPTF EAKAEALHYF
PIWRTWFSLH GLCKLPWNDI IPESNKTAKE PAKVPEHVEN YTWLYEGVTG VKVGIEDLML
QSERVYTFQR IFNARCGYGT RAYDYPPYRA MGPVTELEYE SRQERYDQSL INDAGINIDG
MSTAEKVAAL RKYREDRYEM LVDAVYKRRG WDMNGVPTLE TVKRLGIDFP EVLEVIQKHH
KS
//