ID A0A0S8BLD6_9CHLR Unreviewed; 620 AA.
AC A0A0S8BLD6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 19.
DE RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN ORFNames=AMJ56_05830 {ECO:0000313|EMBL:KPK11675.1};
OS Anaerolineae bacterium SG8_19.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK11675.1, ECO:0000313|Proteomes:UP000050892};
RN [1] {ECO:0000313|EMBL:KPK11675.1, ECO:0000313|Proteomes:UP000050892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_19 {ECO:0000313|EMBL:KPK11675.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK11675.1}.
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DR EMBL; LJNN01000052; KPK11675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8BLD6; -.
DR PATRIC; fig|1703386.3.peg.3194; -.
DR Proteomes; UP000050892; 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 1..183
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 620 AA; 69558 MW; B192295F7B575EA8 CRC64;
MPFGGRAMAS RIAWDEIPAG TTPYDPENRV IVATGPLTGT LAPTTGRTVM TSISPRIYPR
PWYTHSTLGG WFGPEMKYAG YDAIVIHGRA SCPVYLEIQD EKVRLVDAQD LWGLDARETQ
LTLKGRMGSQ GSKIQVLTIG PAGENLVRFS SVQHAEENAA AHSGFGAVWG SKNLKAIAVR
GTGGVSVADP DALLREVLKE EGDRYSLFIT CLFEDGAKKK RPVCSQACIF NCLVSNYGHT
VDGRRVPGQC VGGVAWMSED FMKHTQYSGG GVEIPPSKNF GLCEETSLHE LCNSLGLDLW
FRVVMQPWFI RCKQLGIHQI RGHPIEPNDL FWFEDFMHRL ARREGLGAIF ADDLVRAMDE
LEGELPEELI HLGRELEFDF GFPAHREGRF WDEEPLPFWV ISAMMHASTS RDPTIGAHHS
SLLLAEFLMV DRDVALQQFR ILSQQIWGYP DALEPTFENK APVAIWSQHQ HMLIDSLPLC
DFAFPQLVRP IDTLETWRKT EHIVGDLDLD LRLFAAVTGR EKNHQEMERV AERAFTLERA
MLARAGRDRK MEEAVLAPHF KLPCRADGTL IDEAGFAGLL DEYYSARGWD LELGWPQTDQ
LKALGLNDVI PELDGYRQNQ
//
