FOR_THELN
ID FOR_THELN Reviewed; 621 AA.
AC Q56303; H3ZJK8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Tungsten-containing formaldehyde ferredoxin oxidoreductase;
DE EC=1.2.7.5;
GN Name=for; ORFNames=OCC_05029;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=7642512; DOI=10.1128/jb.177.16.4817-4819.1995;
RA Kletzin A., Mukund S., Kelley-Crouse T.L., Chan M.K.S., Rees D.C.,
RA Adams M.W.W.;
RT "Molecular characterization of the genes encoding the tungsten-containing
RT aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and
RT formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis.";
RL J. Bacteriol. 177:4817-4819(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [3]
RP PROTEIN SEQUENCE OF 1-26, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP AND CHARACTERIZATION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=8390467; DOI=10.1016/s0021-9258(19)38690-9;
RA Mukund S., Adams M.W.W.;
RT "Characterization of a novel tungsten-containing formaldehyde ferredoxin
RT oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis.
RT A role for tungsten in peptide catabolism.";
RL J. Biol. Chem. 268:13592-13600(1993).
CC -!- FUNCTION: Catalyzes the oxidation of C1-C3 aldehydes. Involved in
CC peptides fermentation.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:8390467};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:8390467};
CC -!- COFACTOR:
CC Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC Evidence={ECO:0000269|PubMed:8390467};
CC Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC cofactor per subunit. {ECO:0000269|PubMed:8390467};
CC -!- ACTIVITY REGULATION: Inhibited by arsenite, iodoacetate and cyanide.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 mM for formaldehyde {ECO:0000269|PubMed:8390467};
CC Vmax=17.5 umol/min/mg enzyme with formaldehyde as substrate
CC {ECO:0000269|PubMed:8390467};
CC Note=Significant activity only with aliphatic aldehydes up to C3 and
CC only at high concentration (15 mM).;
CC pH dependence:
CC Optimum pH is above 10 (at 80 degrees Celsius).
CC {ECO:0000269|PubMed:8390467};
CC Temperature dependence:
CC Optimum temperature is above 90 degrees Celsius (at pH 8.4).
CC {ECO:0000269|PubMed:8390467};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8390467}.
CC -!- MISCELLANEOUS: A low amount of aldehyde ferredoxin oxidoreductase
CC activity has been observed.
CC -!- SIMILARITY: Belongs to the AOR/FOR family. {ECO:0000305}.
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DR EMBL; X83963; CAA58795.1; -; Genomic_DNA.
DR EMBL; CP006670; EHR79871.1; -; Genomic_DNA.
DR RefSeq; WP_004066104.1; NC_022084.1.
DR AlphaFoldDB; Q56303; -.
DR SMR; Q56303; -.
DR STRING; 523849.OCC_05029; -.
DR EnsemblBacteria; EHR79871; EHR79871; OCC_05029.
DR GeneID; 16548761; -.
DR KEGG; tlt:OCC_05029; -.
DR HOGENOM; CLU_020364_1_0_2; -.
DR OMA; AHHKDAW; -.
DR OrthoDB; 9593at2157; -.
DR BRENDA; 1.2.7.B2; 6302.
DR SABIO-RK; Q56303; -.
DR Proteomes; UP000015502; 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; -; 1.
DR Gene3D; 1.10.599.10; -; 1.
DR Gene3D; 3.60.9.10; -; 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 Pfam; PF01314; AFOR_C; 1.
DR Pfam; PF02730; AFOR_N; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF48310; SSF48310; 1.
DR SUPFAM; SSF56228; SSF56228; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Tungsten.
FT CHAIN 1..621
FT /note="Tungsten-containing formaldehyde ferredoxin
FT oxidoreductase"
FT /id="PRO_0000087325"
FT BINDING 284
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 621 AA; 68941 MW; 95589C2DC4F18E13 CRC64;
MKGWWGKILR VDLTNNKVWV QEYSPEVAKN FIGGRGLAAW ILWNEAKNVD PLGPKNKLVF
ATGPFNGLPT PSGGKMVIAA KSPLTGGYGD GNLGTMATVH LRKAGYDALV VEGKAKKPVY
IYIEDDNVSI LSAEGLWGKT TFETERELKE IHGKNVGILS IGPGGENLVK YAVVISQEGR
AAGRPGMGAV MGSKKLKAVV IKGTKEIPVA DKEKLKELSQ EAYDAILNSP GYPFWHRQGT
MAAVEWTNEN SALPTRNFSD GSFEFARSID GYTMEGMKVK QRGCPYCNMP CGNVVLDAEG
QESELDYENV ALLGSNLGIG KLNEVSVLNR IADEMGLDTI SLGVAISYVM EAKEKGIIKD
DDAPEFGDFK KAKQLALDIA YRRGELGNLA AEGVKVMSEK LGAKDFAMHV KGLEVSGYNC
YIYPAMALAY GTSSIGAHHK EAWVIAWEIG TAPIEGEKAQ KVEYKITYDP EKAAKVIELQ
RLRGGLFEML TACRLPWVEV GLSLDYYPKL LEAITGVKYT WDDLYKAADR VYALMRAYWV
REFNGNWSRE MDYPPERWFK EGLKSGPYKG QHLEKDKYDA LLSEYYKLRG WDERGIPKKE
TLKELNLEFV IPELEKVTKL E
