ID A0A1F8RHL8_9CHLR Unreviewed; 617 AA.
AC A0A1F8RHL8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=A2W34_04565 {ECO:0000313|EMBL:OGO47169.1};
OS Chloroflexi bacterium RBG_16_64_32.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797658 {ECO:0000313|EMBL:OGO47169.1, ECO:0000313|Proteomes:UP000179752};
RN [1] {ECO:0000313|EMBL:OGO47169.1, ECO:0000313|Proteomes:UP000179752}
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:OGO47169.1}.
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DR EMBL; MGNZ01000076; OGO47169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8RHL8; -.
DR STRING; 1797658.A2W34_04565; -.
DR Proteomes; UP000179752; 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..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
FT REGION 551..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 66816 MW; 89C2E39699D45D96 CRC64;
MLNNAINGKI LNVNLSSGVM EAESLPEEMY RNYIGGYGIG ARLLFDRIPS GADALGPDNI
LGLFPGLLTG TPLFGSRFQV VAKSPKTGGW GDANCGGDFG PFLKHAGWDG LMITGASEQP
VYLLIEDEKT EIKDASDLWG VDAITTEDTL KERHGKKASI ACIGPAGENL SYMAGICNER
GRLAARSGLG AVMGAKKLKA VVTLASRKIL AGDDKEIRAL VRTSLDEFGP AANFFRTFGT
TGITPVSAMS GDSPVKNWGG AGTVDFPQLQ ELSGDKFNAK MDRSYACWHC PLACGAESNE
SENPTYPYPK HTHRAEYETA CSFGTLSLNA DIDSLQYANH LCNAYGLDTI SAGATIAFAI
ECYENELIGS EDTGGLELTW GNNEAIIEML HRIGKREGIG DLFADGIRKA AEKLGPKAEP
FAMDVGGEEL PMHDAKLQPE YFTTYKLDPT PSRHTLYEGA ARAGWAVPPT AKTRNEFSGR
GEHHKGAAEY MHIVNSIGAC MFITFTGPNE RIPEWINAVT GWDVTHDELR RTGERIANLR
MAFHVREGDN PAQRRVPGRL VGSPAQEVGP HKDYTVDGDT MQREYLAACD WDQETCMPSR
AKLTELGLED VARALHG
//