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Database: UniProt
Entry: D1B9T3_THEAS
LinkDB: D1B9T3_THEAS
Original site: D1B9T3_THEAS 
ID   D1B9T3_THEAS            Unreviewed;       731 AA.
AC   D1B9T3;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ACZ19036.1};
DE            EC=1.2.7.5 {ECO:0000313|EMBL:ACZ19036.1};
GN   OrderedLocusNames=Taci_0803 {ECO:0000313|EMBL:ACZ19036.1};
OS   Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS   (Selenomonas acidaminovorans).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19036.1, ECO:0000313|Proteomes:UP000002030};
RN   [1] {ECO:0000313|EMBL:ACZ19036.1, ECO:0000313|Proteomes:UP000002030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49978 / DSM 6589 / Su883
RC   {ECO:0000313|Proteomes:UP000002030};
RX   PubMed=21304665; DOI=10.4056/sigs.40645;
RA   Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA   Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT   "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT   (Su883).";
RL   Stand. Genomic Sci. 1:254-261(2009).
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; CP001818; ACZ19036.1; -; Genomic_DNA.
DR   RefSeq; WP_012869551.1; NC_013522.1.
DR   RefSeq; YP_003317318.1; NC_013522.1.
DR   AlphaFoldDB; D1B9T3; -.
DR   STRING; 525903.Taci_0803; -.
DR   EnsemblBacteria; ACZ19036; ACZ19036; Taci_0803.
DR   KEGG; tai:Taci_0803; -.
DR   PATRIC; fig|525903.6.peg.804; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_0; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000002030; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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,
KW   ECO:0000313|EMBL:ACZ19036.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002030}.
FT   DOMAIN          21..248
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   731 AA;  82818 MW;  BEADB78C75020BC7 CRC64;
     MEKMKLLAQW TYTPKPIHRG YTKEVCLVDL GNRDGKYRFE TKTLSDEFVE RFTGGRGFGL
     GLLWEAVNEN TKWDDPENEI IISGGPLCGI TQYPGAGKCY SVFLSPATKQ TYASNAGGYF
     GPLIKFSGFD SFELRGIADR NVIIFVDGDQ GKVEIYESPF SPKDNSYTIT DELHDYFSAE
     DEDRENGKRA ISVVSTGQAA AHSYICGMNF SFYDLRRKVA RLKQAGRGGG GTVLRHKGVH
     ALVVKKRKVT GVENDPADLA TLQQVGIKLH KEIHDYDDVQ CKMRKVGTAH LNEVMNDYHL
     LPVNNYKFGQ HPDINNIHSD VYTSLFTQGL PDGCWYGCSL SCAKAADNFE LKTGPWKGKK
     VTVDGPEYET AASLGSVIGI FDPKWTIEAN FYADHYGFDT ISLGTILAFL AECYELGLIN
     KDHTGGLELT FGNKDAMMEM IHRMAEGTDE FAVAASRGIR YLKDFLSEKY GADRKVMEDI
     GMEGQGLEVS QYRCQESIAQ WGGYFLTLKG PQHDEAWLIF MDMVNKQLPT FEDKAEALYY
     FPNFRLWFSL VGLCKLPWND IEPADNHIRY KGIEAAKVPE HVQNYVDIFN AVTGKNITKE
     DIITQSEKVY NFERVFNLRM GKGTREWHNI PARGLGPVFE DEYMARPDYF DDKLREAGID
     PQGLSVKEKI EKLQAHRRAQ WEKLVDAVYK RRGWNKNGIP TLETVKRLGI DTPEVVEVLK
     KHLRPEDEWD N
//
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