ID V4XBC2_9ARCH Unreviewed; 610 AA.
AC V4XBC2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN ORFNames=A07HR67_00151 {ECO:0000313|EMBL:ESS05169.1};
OS uncultured archaeon A07HR67.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412871 {ECO:0000313|EMBL:ESS05169.1, ECO:0000313|Proteomes:UP000030660};
RN [1] {ECO:0000313|Proteomes:UP000030660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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; KI543154; ESS05169.1; -; Genomic_DNA.
DR AlphaFoldDB; V4XBC2; -.
DR STRING; 1412871.A07HR67_00151; -.
DR PATRIC; fig|1412871.3.peg.154; -.
DR Proteomes; UP000030660; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000030660}.
FT DOMAIN 5..201
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
FT REGION 270..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 63418 MW; B868A0B1C66449BA CRC64;
MDPPDRILRV DLSTRTVASD PVPDEWLGAY VGGKGLGARY LYAAGGGIDP ESPANTLAFM
TGPLTGYTPG EQRYAAITKS PLTGAFLDSY GGGAFPARLA GSLGSHLGVL VTGAADEPVV
LSLSGGEARV EPADDCWGLD TAETADRFPA SAVACIGPAG ERAVRYATIA SDGGDHHAGR
GGAGAVMGTK RLKAVVARDP PPEPTEELAA LEQRDGSAFA DSDAGRWLAA SDTLETVDFA
NEAGVLPTRG WQERRFEGTE EIGIERATER ATGRERADDP VPGGFRVPSG DGDETDEAAD
TVPRGATPIV LGAGLGIDDF DAVAALGGLC DRLGMDVISA GNAVAWAVRA GDEGVIDRDI
SFGDGKAARS VIAEITARET PLGDALADGV AAAAERFGGT DLIPTVKRMA LSSYDPRGAA
SMALAYATSD RGGCHRRARP VEGDTTAPRP RDPDDVAAAV AAEQDRRAAL WCLIADDFLD
GVFDPSVAAE WLRARGYDHD ATSLSGLGER VWTLVRLYNL REGFGRDDDA LPAAIAGAPG
GEEAPGSTAD EPTNRPPGLD PEAFENLLDR YYAVREWDAA GRPTDDLLER LGLAGLADDP
ISPNERTDPG
//
