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Database: UniProt
Entry: A0A0S8HWM8_9DELT
LinkDB: A0A0S8HWM8_9DELT
Original site: A0A0S8HWM8_9DELT 
ID   A0A0S8HWM8_9DELT        Unreviewed;       334 AA.
AC   A0A0S8HWM8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   28-JUN-2023, entry version 17.
DE   RecName: Full=Aldehyde ferredoxin oxidoreductase N-terminal domain-containing protein {ECO:0000259|SMART:SM00790};
DE   Flags: Fragment;
GN   ORFNames=AMJ94_12605 {ECO:0000313|EMBL:KPK89281.1};
OS   Deltaproteobacteria bacterium SM23_61.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK89281.1, ECO:0000313|Proteomes:UP000051218};
RN   [1] {ECO:0000313|EMBL:KPK89281.1, ECO:0000313|Proteomes:UP000051218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_61 {ECO:0000313|EMBL:KPK89281.1};
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   -!- 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:KPK89281.1}.
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DR   EMBL; LJUR01000124; KPK89281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8HWM8; -.
DR   STRING; 1703399.AMJ94_12605; -.
DR   PATRIC; fig|1703399.3.peg.1576; -.
DR   Proteomes; UP000051218; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR   InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
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;
FT   DOMAIN          5..207
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
FT   NON_TER         334
FT                   /evidence="ECO:0000313|EMBL:KPK89281.1"
SQ   SEQUENCE   334 AA;  35656 MW;  8CDAA87EDC21F591 CRC64;
     MPFGYMGKIL RINLADKDIR VEDIRQDWAE QFIGGPGLAT RYLYDEVPKG GDPLGPENKL
     IFMTGPLTGT ASASAGRYSV VAKSPLTGIW GHANSGGSFG PALKRSGFDG IILEGVASRP
     LYLTIVDGQA ELHDAGGLWG RTVAETEDMI QQQTGEKKLT MASIGPGGEN RVRYAAIMNN
     SHRAAGRCGL GAVMGAKRLK AIACGGNASV ALAEKDTFNE VARKQYELLD ESMLKVGFET
     FGTNMVSDMV NARGGYPTRN WQQGVFDQIE NVNSQALTDK VFVRGVKCFA CPIACGRGSE
     IKEGKWAGRK GEGPEYESAV TLGAMCGVSD MNAI
//
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