ID A0A0F2JFW1_9FIRM Unreviewed; 656 AA.
AC A0A0F2JFW1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Tungsten-containing aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:KJR48176.1};
GN ORFNames=UF75_1428 {ECO:0000313|EMBL:KJR48176.1};
OS Desulfosporosinus sp. I2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR48176.1, ECO:0000313|Proteomes:UP000033442};
RN [1] {ECO:0000313|EMBL:KJR48176.1, ECO:0000313|Proteomes:UP000033442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I2 {ECO:0000313|EMBL:KJR48176.1,
RC ECO:0000313|Proteomes:UP000033442};
RA Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V., Ravin N.V.;
RL Submitted (FEB-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:KJR48176.1}.
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DR EMBL; JYNH01000017; KJR48176.1; -; Genomic_DNA.
DR RefSeq; WP_045573826.1; NZ_JYNH01000017.1.
DR AlphaFoldDB; A0A0F2JFW1; -.
DR PATRIC; fig|1617025.3.peg.1481; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000033442; 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:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE: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:UP000033442}.
FT DOMAIN 6..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 656 AA; 75135 MW; 215D4E1BBFB6CB9F CRC64;
MRCAETGYNL EIDLATGNIE KVETDPKLTE LHLGGLGYNV KLFWDRVPPE TKAFDPENLL
IFSSGLLCGT PAFSFNRTCV TTISPQTELL AYPMMGGFWA AELKYAGYDR VIFRNKSPKL
VYIYINNDKV EIRDASHLKG MGTVEIRDIL KKELNEPKVS IAAIGLAGEN RVFTASIEQG
RSSASRLGGG AVMGDKNIKA VVVRGTKDIN LARGEEFIKH VNKVGEYIKF RNENPLKGVM
TILSGIGSPQ EMKHTDEKWH TENFSWGNAR TRRRDFWTDE INQSWSSTQR AAIKRYISCF
NCPQQCGALI SYKDVPRFKQ KCFTKLTYSM AAYVDNLEFN FRIAQRATEY GVDGFSTPQI
LAFAVELYEA GILTDKDFEG CPPDKEGRFN WLLDRVVRRE GIGDILADGT YWAARRIGKG
AEAFDHNTIK KHEQLPLKLG MMDPLYFLMY STNEKISITQ IEGNWPQAPF PTKEMREEFV
KDWPQLPDDH FKQYFLDWEP RGENSNPYYP TPDMCSEIVD WMEEIHNIDD ALGLCCGMGS
FCLKPPYHTH NYHLLVSSAT GLDIDQVGLK KIVNRSRNLH RAYNVLKGMR RADEKPPQDH
WKKRFPELEE QLLDTYYKYK GWNMEGIPTK EKLLELDLDY VAEDLERRGI LKDGQN
//
