ID Q9HJ31_THEAC Unreviewed; 623 AA.
AC Q9HJ31;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN OrderedLocusNames=Ta1142 {ECO:0000313|EMBL:CAC12268.1};
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075 {ECO:0000313|EMBL:CAC12268.1, ECO:0000313|Proteomes:UP000001024};
RN [1] {ECO:0000313|EMBL:CAC12268.1, ECO:0000313|Proteomes:UP000001024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165
RC {ECO:0000313|Proteomes:UP000001024};
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.L., Koretke K.K., Volker C.,
RA Mewes H.W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a
CC carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:16421, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001714};
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; AL445066; CAC12268.1; -; Genomic_DNA.
DR RefSeq; WP_010901550.1; NC_002578.1.
DR AlphaFoldDB; Q9HJ31; -.
DR STRING; 273075.gene:9572364; -.
DR PaxDb; 273075-Ta1142; -.
DR EnsemblBacteria; CAC12268; CAC12268; CAC12268.
DR GeneID; 1456646; -.
DR KEGG; tac:Ta1142; -.
DR eggNOG; arCOG00709; Archaea.
DR HOGENOM; CLU_020364_1_0_2; -.
DR InParanoid; Q9HJ31; -.
DR OrthoDB; 30771at2157; -.
DR Proteomes; UP000001024; 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: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:UP000001024}.
FT DOMAIN 4..205
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 623 AA; 68316 MW; 4026BC3610ED6935 CRC64;
MYGFNGKILW ADLTNEKMWV EEIPEDIYKK YLGGVGLGAY ILNREIKGNI DALGPDNILG
FITGLFNSHN APLGGRLEVV AKSPMTGTWG DSNCGGKFAP ELKNTGFDAL FVKGIAKRPV
YIKIVDDKYS IEDASNLWGK DAYETETELK KIDPKGQAMV IGVPGEKMLY AAAIMNEYGR
AAGRSGLAAV MGSKKLKGIF ARGTKKIPVY DEKMLMETIK KAQIQFRNSM NLVNPWHMFG
TTQITESSHL NGDTPIKNWA GVGIVDFGEE NAKKISGEEI RKDVLKSYGC AQCTLACGGH
VKRETRYGTV EGHRLEYEGT GAFGGLNLIA DLDAMSMSFE LCNRYGLDII TTGAVIAFAN
ELYERGILTE KDIGFKIGFG NPDAEVKLTE LIGKGEGIGR ILGMGQRYAA KVIGKGAEES
AMEIGGQDLP MHDPRLMPSL GNTYISDATP GRHTAGGIGF NEGFELVLPF KHKDSWTKIP
RYEYHGKAYW QLLSVAGQEI LNSTGMCLFS TNIWPNSYPY TELIKAITGW DMTEDDLVNI
GWRIQIARHV FSAKQGINQY EIKPPGRVMG YPPLKAGPTA GVSIDYETLR NEYLSQLGLA
RDGKPNPEVI KKLGIEPELV AGI
//
