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Database: UniProt/TrEMBL
Entry: R4KLI0_9FIRM
LinkDB: R4KLI0_9FIRM
Original site: R4KLI0_9FIRM 
ID   R4KLI0_9FIRM            Unreviewed;       666 AA.
AC   R4KLI0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:AGL01415.1};
GN   ORFNames=Desgi_1970 {ECO:0000313|EMBL:AGL01415.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL01415.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL01415.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL01415.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) 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}.
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DR   EMBL; CP003273; AGL01415.1; -; Genomic_DNA.
DR   RefSeq; WP_006522596.1; NC_021184.1.
DR   AlphaFoldDB; R4KLI0; -.
DR   STRING; 767817.Desgi_1970; -.
DR   KEGG; dgi:Desgi_1970; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_9; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000013520; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013520}.
FT   DOMAIN          6..207
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   666 AA;  75910 MW;  1FCD964FCCA7A1B6 CRC64;
     MRYAETGYNL EVDLTRGNIE VVQTDPRDTE LYLGGLGTNA KIIWDRVPPE VEPFSPDNLL
     IFSAGLLCGT PATGCNRTIV TSISPQTRLF AYSMMGGFWA PELKYAGYDK VILRGKSPNL
     VYLWINNDKV EIRDASHLKG KGAVETQDLI RQELNEPKAQ VAAIGLAGEN RVYFASIEQG
     RSSCSRQGLG AVMGDKNVKA IAVRGTRDIN IARPAEMIGL INEVLEYIKW RNENPIPNYM
     PILAGLGSPQ EMKHDDEKWH TENFSWGNAR ERRRGFWNEE IAKDWKETMA TMQRRTISCY
     NCPMRCGATI SPPGKSTYMM KCFSKLTYTM AAYLDLEFGL GIAQSATEYG VDGYSCPQVM
     AFALELLEAG ILTDNDFPGM PSDNEGRFYW LLDRIVRREG IGDILANGTY WAAQKIGNGA
     EEFAHNNIKK HEQLPLKLGK LDPIYYLMYC TNEKITITQI EGNFPQAPFM TREEREAFVS
     NWIQVPNERI KQVVLEWEPR GEKSAPYFPT PDMCCEIVDW MERMHYIDDA LGMCAGLSAF
     PLKPPYHIHN YPKIISAASG IEMDEEVLTQ ATKRYRNLVR ANNIIRGMRR KDEVPPEDHW
     KKRFPELEKE LLDKYYKFKG WNNDGVPTKE TLHDLGLDYV AEEFEKRGIY SETPSYEILA
     EKEKEV
//
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