ID A0A0S8HT99_9DELT Unreviewed; 493 AA.
AC A0A0S8HT99;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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=AMJ94_16430 {ECO:0000313|EMBL:KPK87780.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK87780.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK87780.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK87780.1};
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:KPK87780.1}.
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DR EMBL; LJUR01000189; KPK87780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HT99; -.
DR STRING; 1703399.AMJ94_16430; -.
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: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}.
FT DOMAIN 2..89
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 493 AA; 54428 MW; 2E6CD8DBE5D38A04 CRC64;
MYLFIHDGTA EIRDARHLQG KGTFETEEIL RKELNLGFRG SVYGIGPAGE NLVRFAMISG
DGGHVVAHNG MGAVMGSKKL KAIVVARGKA GFAVKDKAAV ERLTRELHED AKTKGSKRIY
EWGTGGGFSA AALGGWLPIK NYTTGIFPEH EKLDGQYIRT HFKMKDNPCW ACQLRHCKLC
EVTEGPYKGF KGEEPEYEGL AAWGSVIGNA DPGATVMLNW FNDQVGMDLN EAGWTVGWAM
ECYEKGVFTQ KDLGGLDLKW GNVGAAKELL KQIAHRQGIG SLLAEGVKRA SEKTGGEAAK
WAIYTHTGAA PRGHDHRGRW CEMLDTCTSG NSTIEATRGG VFPERSGYPP VFDKFSPWEV
AAINAKENGW LPFVDCLGIC AFTCPNRELT VQCVNAVTGW DLDLKGATHI GRRVVNLLRV
FNLRHGLDPK NERPSFRYSE TPKDGPVKGR AIQPHFDFMV RIYRELMGWD PETGRPLPQT
LKSLGLEELI EKF
//
