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Database: UniProt
Entry: A0A0P6XXZ8_9CHLR
LinkDB: A0A0P6XXZ8_9CHLR
Original site: A0A0P6XXZ8_9CHLR 
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}.
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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
//
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