ID A0A1F8Q4I0_9CHLR Unreviewed; 641 AA.
AC A0A1F8Q4I0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN ORFNames=A2Z29_09885 {ECO:0000313|EMBL:OGO30360.1};
OS Chloroflexi bacterium RBG_16_56_11.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797649 {ECO:0000313|EMBL:OGO30360.1, ECO:0000313|Proteomes:UP000177333};
RN [1] {ECO:0000313|EMBL:OGO30360.1, ECO:0000313|Proteomes:UP000177333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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}.
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:OGO30360.1}.
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DR EMBL; MGNQ01000053; OGO30360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8Q4I0; -.
DR STRING; 1797649.A2Z29_09885; -.
DR Proteomes; UP000177333; 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 6..208
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 641 AA; 69904 MW; A689D400989F1372 CRC64;
MPDYGYAGEI LKVDLSNGKI QRQPSSNYTD KYIGGHGLAA RLYWEMVPPE AKAADPENCL
ICASGPLAGF SGFAGSRWKI CGKTPLGDPE SFSYCNLGER WGTVLKYAGY DALAVQGRSD
KLAYIYIHDG QVEIRDASHL RGLTTLDTGD SLKSELGKGV SVLSIGPAGE NMVPFSIVLA
EGGASGSGGV GAIMGSKNLK AIVVAGDKKP SAADPDRVNK LAEVIRVNRP RIDMPSMWGV
PGLTHRHACY GCGIGCSREV YKDEKGRENK ALCQASAVYA APSQRYTGKN DGAHLLGTRL
CDGYGLDSSV MQSMIEFLEA CYEEGLVDEN KTGLPLSKIG GPEFIETLTR KIAFREGFGE
VLARGIVASA AALGQAATQM LHRFIATPGS EKKDYDPRLF ITTALFYATE PRRPIQQLHE
VCSMVMMWLG MGPNSRPGAM FSTENFRRFA EMAWGGAVAA DFSTYEGKAL AAKKIQDRVF
AKESLVICDL RWTMTETARI LGTTGDNVME SQVYSAVTGK ETDDAGLYRL GERIFNLQRA
ILLREGRPGR DGDRLLDYFF TEPLKKGELF FDVDALAPGR DGEIISKVGA VLDREKFENM
KTEYYRHRGW DAASGFPTRT TLRSLELEDV AADLQNRGLV H
//