ID A0A0N8I0E3_9EURY Unreviewed; 380 AA.
AC A0A0N8I0E3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN Name=aor_5 {ECO:0000313|EMBL:KPN32067.1};
GN ORFNames=SY89_02825 {ECO:0000313|EMBL:KPN32067.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN32067.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) 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 -!- 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:KPN32067.1}.
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DR EMBL; LGUC01000001; KPN32067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8I0E3; -.
DR STRING; 699431.SY89_02825; -.
DR PATRIC; fig|699431.3.peg.2887; -.
DR Proteomes; UP000050535; Unassembled WGS sequence.
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:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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 InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
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 SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:KPN32067.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535}.
FT DOMAIN 48..369
FT /note="Aldehyde ferredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01314"
FT REGION 360..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 41311 MW; BDAA7961AD8944F7 CRC64;
MTFDSRAFGR GGIGAILGSK NVKCVTFEGD SAPEIEIADP PASDVHREAA TSDDLMRRQG
TTGNTEFIND NFSIPTRYFD DYEFESIENI GGNAVEEKKY KKGACSQCAY ACKLPTKDEE
RGVETEGPEF ETVYSFGTCQ GVDDIVDVMI SNELCDELGM DTISAGVTVA AYLKSEDAFG
DAELVHETLE KIAYREGIGD TLAEGTARAH EELGVDNYTV KGMEFAAHDG RTLHGQGLSY
AVANRGADHM YGGMLGLEYS GEVDPEGTLG KAETLVGLEN HNVVRDSGVV CAFGGDYLTD
ERLETLLDAD YEELQEVGAR TVERERHFNN KRGKDVADDN LPYEIPDLAE AVQEYYEARG
WNDDGTVPDA SVDSVAPADD
//
