ID A0A0S8HUC3_9DELT Unreviewed; 622 AA.
AC A0A0S8HUC3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
GN ORFNames=AMJ94_15445 {ECO:0000313|EMBL:KPK88306.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK88306.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK88306.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK88306.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK88306.1}.
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DR EMBL; LJUR01000170; KPK88306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HUC3; -.
DR STRING; 1703399.AMJ94_15445; -.
DR PATRIC; fig|1703399.3.peg.2418; -.
DR Proteomes; UP000051218; 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 8..211
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 622 AA; 67636 MW; AA5CF283BAC00C2E CRC64;
MNDTICGYHG KVLRANLSKG TFTTEPIDER FCRKYLGGAG FISYYLWKEL PQGIDPLGPD
NKLIFALGTA TGFPLAGSGR HCVGAKSPLT GGIAKSEPGG FWGAELKRAG FDAIIVEGKA
PEPVYLWIHD GDVSLRKASQ IWGQDTKETE QAIRDELGDQ KIQLALIGPA GENLVRYSVV
MHGLFDAAGR GGTGAVMGSK NLKAIAVRGR KLPSSAKPEG IKELREWLSN NMNLVKGYRD
FGTSGRMIEF EKLGNLPTRN FQDGAFAAIE RISGQTLKAT IGVGMDGCFA CPVRCKKRVA
FQEPYPVDPD YGGPEYETQG ALGSNCGVED LKAISLASQL CNAYSLDVIS TGCTIAFAME
CFENGLLTSK DTGGIELRFG NAEAMLQTIK LIAKREGIGN LLAEGSARAA EQIGQGAEAL
AIHVKKQEIP MHEPRLNKAL GLGYMVNPHG ADHCCNMIDI LFNGLSSTAD IVLKDMIPLG
WVEPVPLDDI SPPKVSLFRM LHLKRIAFDS LGICQFLPYS FQQVADLASA ITGWDIGPMG
LARVSERVLT LYRLFNIREG FSADDDKLPK RFFHPTKYGP LAHTALDPEK MERAKRYYYS
LMGWDANSGK PMPETIEALG II
//
