ID A0A0M0BH18_9ARCH Unreviewed; 615 AA.
AC A0A0M0BH18;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=AC480_04460 {ECO:0000313|EMBL:KON27674.1};
OS miscellaneous Crenarchaeota group archaeon SMTZ1-55.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1685133 {ECO:0000313|EMBL:KON27674.1, ECO:0000313|Proteomes:UP000037456};
RN [1] {ECO:0000313|EMBL:KON27674.1, ECO:0000313|Proteomes:UP000037456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMTZ1-55 {ECO:0000313|EMBL:KON27674.1};
RA Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA Teske A.P.;
RT "New insights into the roles of widespread benthic archaea in carbon and
RT nitrogen cycling.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KON27674.1}.
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DR EMBL; LFWX01000074; KON27674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0BH18; -.
DR PATRIC; fig|1685133.3.peg.578; -.
DR Proteomes; UP000037456; 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; 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; 2.
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}.
FT DOMAIN 5..221
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 615 AA; 67790 MW; BB9ECEB28B4F9943 CRC64;
MSRGYAGKWL DVDLTQETID EITFPEKTLR QYIGGRGLAA KVLWDRLGTQ WADVDPLGPQ
NVLTILTGPL TAIHPGTRIC VSGKSPISNG VVGSTASSEF AAELKCAGYD GLLISGKASS
PVYLLVTDDG AEIRDAAHLW GKVAEDTLKI LNQEVAAELT RRKSEVGLWK EPAMVYIGPA
GENLVRNAAV VTKLVHAAGY GGYGAVMGSK NLKAVAAKGR GPLPEVAAPK TVEILWREYH
RRLIAMDRMR RWGTGYAGWE TGAVTSSEPV RNWQEEWHDE RSMAGPRYSS RFWVKAYWAD
FNCSRSCMKI SCIKSGRWKG DITDMPDYEL EAYCGTNLGL FDPGDNIHIS ALIDNLGMSG
INTANTLGFA AELYQRGILT EEDLGFALEW GDAEAFTKLA WLIVNREKIG DVLAEGTYRA
AQKISEMKGV DVMPYAVHVK GIEIGAHGTR SNEDYTKDMC YAASTQGGDH TSVVRDAYND
MGTVFMDSAV VCMFCVVQDL VWDYARAVTG WDITQHTWST EQGPRIQTLQ RALLLLGGPD
VFWDPDTDDD NPPRFYEPLP TGPYKGRTTD AAVVEQNKQD YFSAIGWDAR GIPTTQTLER
LDLQDLEAVM KPLRK
//
