ID A0A0N8GPK4_9CHLR Unreviewed; 713 AA.
AC A0A0N8GPK4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:KPL81146.1};
GN ORFNames=ADN00_00840 {ECO:0000313|EMBL:KPL81146.1};
OS Ornatilinea apprima.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Ornatilinea.
OX NCBI_TaxID=1134406 {ECO:0000313|EMBL:KPL81146.1, ECO:0000313|Proteomes:UP000050417};
RN [1] {ECO:0000313|EMBL:KPL81146.1, ECO:0000313|Proteomes:UP000050417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3M-1 {ECO:0000313|EMBL:KPL81146.1,
RC ECO:0000313|Proteomes:UP000050417};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Ornatilinea apprima DSM 23815.";
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 -!- 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:KPL81146.1}.
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DR EMBL; LGCL01000002; KPL81146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8GPK4; -.
DR STRING; 1134406.ADN00_00840; -.
DR PATRIC; fig|1134406.4.peg.3566; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000050417; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050417}.
FT DOMAIN 22..240
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 713 AA; 80189 MW; 558B00E4856DCE88 CRC64;
MSEQREIIQQ YSYETRAVHQ GYANRTLYIN LSSSEIKERP VTQQMKDIFT GGRGFCLWLL
WNAVSEKTQW NDPENELILA SGPIGGIIQY PGSGKTTVVT LSPLTHNVYD SNGGGYFGPY
LKFSGWDAME IQGKANEDVI LFIDGDTGTV QIESAGDLPS DTHLLSEMLT GQYAGSEENM
RNISVVSAGQ GAENSLLGGL NLSFYDNKRG EIRYKQAARG GVGHVFRDKK IKAIVVKYSH
LSASSNGPAK PELIRDAGRR INQEILGLDN KQNNMRTLGT TNLVEIINHT DLLPTENFRY
GSDPRAKMIS AEYWRDVFDH TSQDSCWYGC SMACAHKVND FVLKSGPYKG QKVLVDGPEY
ETIGGMGSNI GVFDPEALLE FNFYCDTYGL DTISMGSSIA FAMECYEVGI LDQQVTGGLD
LTWGNSDAVL EILHQIARGS GFGLVIGRGI REMKKIFAEQ LHADPQFLQD IGMEIKGLEI
SEYMPKESLA QQGGFALANK GPQHDEAWLI FMDMVKNQIP TFEDKAEALH FFPVFRTWFS
LHGLCKLPWN DIIPEDNYLE KEPAKVPSHI RNYLALYEGV TGTPITQKEL LEQSERVYNF
QRIFNLRMGT GTRAHDYPPY RAVGPVTEKE YLSRVERYDR DLREKVGVDP DKMTLEEKIL
TLRRYRMDQY EQLVDAVYKR RGWDHDGVPT LETVRRLGID FPDVVALIKA HGG
//
