ID A0A135VBU5_9ARCH Unreviewed; 1207 AA.
AC A0A135VBU5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=AM326_00925 {ECO:0000313|EMBL:KXH70137.1};
OS Candidatus Thorarchaeota archaeon SMTZ-45.
OC Archaea; Asgard group; Candidatus Thorarchaeota.
OX NCBI_TaxID=1706443 {ECO:0000313|EMBL:KXH70137.1, ECO:0000313|Proteomes:UP000070599};
RN [1] {ECO:0000313|EMBL:KXH70137.1, ECO:0000313|Proteomes:UP000070599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ-45 {ECO:0000313|EMBL:KXH70137.1};
RX PubMed=26824177;
RA Seitz K.W., Lazar C.S., Hinrichs K.U., Teske A.P., Baker B.J.;
RT "Genomic reconstruction of a novel, deeply branched sediment archaeal
RT phylum with pathways for acetogenesis and sulfur reduction.";
RL ISME J. 0:0-0(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH70137.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LRSM01000196; KXH70137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135VBU5; -.
DR Proteomes; UP000070599; Unassembled WGS sequence.
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; 3.30.300.30; -; 1.
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 Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_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 Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR PROSITE; PS00455; AMP_BINDING; 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}.
FT DOMAIN 1..207
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 1207 AA; 133847 MW; F590750EB06B69AD CRC64;
MGKILRINLT TSTITEEFPD EGTLRKYLGG SGLATKILFD ETEPGIDPLG PENKLIFMTG
PLTGTTSPST GRYSVVTKAP LTNGWGHANS AGFWGRDFKR SGFDGVIFEG KASKPVYLLT
QDGKAELLDA SEIWGKNTSE ATRILREKHG DKFNVACIGI AGENLVKYAA IMNDCDEENW
GRAAGRCGVG AVMGSKNLKA IASMGTMIIP IAEPEAYRDE AKQRFDWVNQ SILKMTLEVY
GTATMVDLVN VKGGIPTRNW QTGVFENAEK INGTAINDSI LVKRKPCFAC PIHCGRIAEI
KTGPFKSKGE GPEYETLSSF GTMCGVDNLE AITLAHFLCN EYGIDVISAG NTVGFAMECY
QRGILKDEDV DGMDFSWGNA QLIVDIVHKI GRREGVGNLL AEGTKRMSEK LGQGSEKFAM
HVKGLELPGY DSRAAKVTGL AYAVANRGGD HITAYIEGPA FLAMPFMIVE DADVGDPLEE
IPETALVVKN FEDALGNFDA IGGCKFMGMV LTADDWAGLM SSLMGIDITA DEFRKTGERI
YNLERAYILR EGFTGADDTL PARLLEDPLP EGPAEGQVVN LDVLLDAYYK YRGWDEQGRP
TKEKLQELSL EWLIPTVHED AAYVKEVTRH KVQPITAPVK KDVPQMKAQE VMGEEPWFNS
YQIGPFKLEH SMAPYPEVNV YKFLEDTARE FPDVVACIYA DEEMMYPELK DKVDRLASAL
VALGVKKGDA VATVLPSCPE FIIADYAAMK IGAIHVPLSI LHKKDDLKYE LNESNAEIVV
CSYRRIERVN QIKSETKVKT VIYAPTKLFP DYEYPEMEDI EDDNYYLLND LIEMHEPHTE
TVEINPKEDI ALLPFTGGTT GQPKGTMLTH YNITSNVRQT MHWMMDPLKE GIIGKSAGVI
CVPIFHAYGH WALHACISWG IKMYLMDSRD IPKIVDVINR HRPFTVFAVP THYMLFSKMD
LIKGQIFYFS GAAALPVDLA EEFEEKSGVP MGEGYGATET SGVVTINISA LSKVTGFMAE
TKRGVGIPVP ETEIKIVDQD TGKELPIGER GEIWIRGPQI MKGYWPTPGS GLKEGGWLPM
GDVVEMDSDG YFKVVDRIKD MINVSGNKVY SRVIDDILHE YEAIDIAGVI GIPDPERPGS
ERVKAFIQLK PEYRGKVSEQ EIIDFLKDKV KPYAIPKWVE FRDELPLTVV MKLFKKKLRE
EELAKLS
//
