ID A0A1F8KRV8_9CHLR Unreviewed; 608 AA.
AC A0A1F8KRV8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:OGN76466.1};
GN ORFNames=A2X25_09635 {ECO:0000313|EMBL:OGN76466.1};
OS Chloroflexi bacterium GWB2_49_20.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN76466.1, ECO:0000313|Proteomes:UP000178842};
RN [1] {ECO:0000313|EMBL:OGN76466.1, ECO:0000313|Proteomes:UP000178842}
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:OGN76466.1}.
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DR EMBL; MGMF01000001; OGN76466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8KRV8; -.
DR STRING; 1797612.A2X25_09635; -.
DR Proteomes; UP000178842; 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 608 AA; 66134 MW; 91837F419F9AA669 CRC64;
MTLGGYANKL AWVNLTAGKV EFKPVPEDLA RKYIGGRGLG VKFVYDNGPK VDPLSPDNIL
CFMNGPLTGS EANMSGRMAV VTKSPLTGTI TDSHHGGWSA ARLRWAGFDG LIFKGKAAKP
TYAYIHDGEL ELLDAKEVWG KGVHDTIKFF KEKYGEKDLS VISIGPAGEK LVKFGCWINE
NDRASGRGGT GCVGGSKNLK AIVIKAEKNL TKAPDREAWK IAHDRALKGI MAPENITSPR
KGGLSVYGTN VLTNIDNNIG AYPTKNSQFT AFGKDAETLS GEWVKENILV NDPTCHACPT
ACKKEVEIKD GPYKGLHMES VEYEPCWSLG ANCGNPDARL VAKMIDLAND YGFDAIEVGH
PLAVWMEASQ RGYTNGDGKL AWGDGDGMTK AAAMIAKREG LGNIMAEGAD ATAKHFGHPE
LAMTCKKQGI PAYDPRGLKG MGLGYATSNR GACHLRAYTP AAELNIMPYG SLKVDPLEWK
GKGGLVKIFQ DIHAFSDSMD LCKFSAFAMG AEEYAQQYAA MTGVPFTTDD VLKTGERIYN
LERHYNNLNG FREGSDTLPR RFLYEPSDQQ GSMGQVCELD KMLVEYYEAR GWKDGVVTEA
KLKELEIA
//
