ID A0A101VA74_9FIRM Unreviewed; 635 AA.
AC A0A101VA74;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:KUO50952.1};
GN ORFNames=APF76_03120 {ECO:0000313|EMBL:KUO50952.1};
OS Desulfitibacter sp. BRH_c19.
OC Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC Desulfitibacter.
OX NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO50952.1, ECO:0000313|Proteomes:UP000053015};
RN [1] {ECO:0000313|EMBL:KUO50952.1, ECO:0000313|Proteomes:UP000053015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO50952.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-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:KUO50952.1}.
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DR EMBL; LOER01000028; KUO50952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VA74; -.
DR STRING; 1734395.APF76_03120; -.
DR Proteomes; UP000053015; 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 5..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 635 AA; 69962 MW; CDF4DE62FB97BFD9 CRC64;
MKYGYTGTIL RVNLSTKIIA KEPLSQELID GFIGGRGFVS KILYDELPLK TDPFSEENML
IIATGPFSGS FLPATGKTHF GTKSPATGGF GDSNMGGHFG PALKYAGYDL LIITGISHEP
CYLFIENDKV EIRSANKYWG KGAIEAEKMF KDELGEDFHS ITIGPAGENK VRISCISHDF
GRQAGRTGVA AVMGSKRLKA VSIKGTGSIP VFDIEGLYKK GKEAYKEITK KPGFLGWTPQ
GTAGITDWCN EAGAFPTKNF QTSYSDHYKE INGQAILDRL KITDKGCFAC PTPCGKYGHT
KTKMGSAYVE GPEYETIALL GGNCYLKTIE DVAYANYICD ELGLDTISGG LAASWAIECY
EKGILTQEDI GREIQFGDLE SVVYLLNKIG HREGIGDLLA DGVKSASAKT GQGSEKFAIH
VKGLEWSGYE CRNAPGMMLA YMTADIGAHH SKAWVLGHDV AGSAANVHDL ISAGAKADKL
PKSTIAGKAE IVINSQHTRP TFDLLGICRL QYMELGFEVE YYEEFFYLMT GKKVSWEELR
TISEKIWNLN RCFNLREIED YGRQYDYPPA RFYEEPVPNG PNEGHFITKE ELDLLLDDYY
KVRGWNKEGK PTKETLERLG ILSLVENTFK SNSSA
//
