ID   B8D3Z4_DESA1            Unreviewed;       650 AA.
AC   B8D3Z4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase-like protein {ECO:0000313|EMBL:ACL10825.1};
GN   OrderedLocusNames=DKAM_0499 {ECO:0000313|EMBL:ACL10825.1};
OS   Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS   1221n) (Desulfurococcus kamchatkensis).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=490899 {ECO:0000313|EMBL:ACL10825.1, ECO:0000313|Proteomes:UP000006903};
RN   [1] {ECO:0000313|EMBL:ACL10825.1, ECO:0000313|Proteomes:UP000006903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n
RC   {ECO:0000313|Proteomes:UP000006903};
RX   PubMed=19114480; DOI=10.1128/JB.01525-08;
RA   Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA   Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Complete genome sequence of the anaerobic, protein-degrading
RT   hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL   J. Bacteriol. 191:2371-2379(2009).
CC   -!- SIMILARITY: Belongs to the AOR/FOR family.
CC       {ECO:0000256|ARBA:ARBA00011032}.
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DR   EMBL; CP001140; ACL10825.1; -; Genomic_DNA.
DR   RefSeq; WP_012608167.1; NC_011766.1.
DR   AlphaFoldDB; B8D3Z4; -.
DR   STRING; 490899.DKAM_0499; -.
DR   GeneID; 7170725; -.
DR   KEGG; dka:DKAM_0499; -.
DR   eggNOG; arCOG05072; Archaea.
DR   HOGENOM; CLU_440510_0_0_2; -.
DR   Proteomes; UP000006903; Chromosome.
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: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;
FT   DOMAIN          6..231
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   650 AA;  74014 MW;  F21EE0DF5CF7AD43 CRC64;
     MNMRRYRALF IDASTRKHWV EEYELNEVYS PISLGLKLHM ERYRSWSKPI YHSDNALILG
     AGLFTGSKMY GVHRFVAVFR SPLTKGLHVS EMGGAAFQFK INADAVVIVG RSETPLIVKI
     YDQGNGEPVV EFHEIQEETL EHVWKGYGGF KGIYALQQYL SDHFKGFYEE FNGRSILVGP
     ASKYTNIGAL ASVTLNKGRM DHGSEDFAAR AGGGSILYRA HGVAAIIYGG RYDRSTKVPK
     ELSDTRELDK LFMELTKQPY TQAVINAGVK YRYDPKLNTG GTLGGNYPHL KATTPMFNWK
     MIYLPKDLRE KLHELIMKYM WEPFNREAIE TRSWKTCGEP CPLACKKVRL GKYKSDYEPY
     NGLGPIIGVL DIHEAEKVVE LADAYGFDAI ELGQIIGFLF EAMDKGLLRP EEIGLPGKPF
     FDPASYSIEH ARVNAELAVK IIEQLAFGSN PLLRLIGERG LRSAAKILDI LYRERTIERK
     TRFSDIPIYA VFGEEGHITP NYYWTPGLVA PLVVLGKYWT VYSGVFMEPE EFASKSIERA
     IYEALIADMG LCRFHRGWAE KAIPVILEKY YGVEKPLEKT RELYKKIAEY QKLAGALPVF
     WDSGKIIDFM AHAAEEYGNV EWGGKFKVNK EAAAREWWER FYRKLEELTS
//