ID A0A0P7FVR6_9EURY Unreviewed; 539 AA.
AC A0A0P7FVR6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN Name=aor_3 {ECO:0000313|EMBL:KPN31084.1};
GN ORFNames=SY89_01826 {ECO:0000313|EMBL:KPN31084.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN31084.1, 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 -!- 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:KPN31084.1}.
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DR EMBL; LGUC01000001; KPN31084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7FVR6; -.
DR STRING; 699431.SY89_01826; -.
DR PATRIC; fig|699431.3.peg.1872; -.
DR Proteomes; UP000050535; 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: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,
KW ECO:0000313|EMBL:KPN31084.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535}.
FT DOMAIN 1..108
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
FT REGION 520..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 58414 MW; BD338E01F2554945 CRC64;
MGRLRRPPVR GKADKPVYAV VEDGEVELRD ASHIWGDGLH DAIDTLEEEV DGAYGKNLSA
MAIGPGGENQ VRYACIINED DRASGRGGTG AVMGSKNLKA VVVKSGTEMP KPADRETFME
GHKAAMQAIQ ESDVTAPNEG GLSVYGTNVL MNLTEEMDGL PTRNGRFTST STEAEKEPDD
LNIDSEKVSG ENVEENILVD DPTCHSCPVA CKKEVEVDVH HKGQDLNVRM ESYEYEPAWA
LGPNSMNDDR DMIAVMMDRC NDLGIDSIET GNILAFAMEA TEKGYIDDAD GIDWGDVDAM
TEMIEKIGQR EGDFADTLAE GQKRAAEALD AHDCRLDVKG QAIAAYDPRG MKGMGIGYAT
SNRGACHLRG YTPAAEILGI PEKVDPTEWE GKGELTAAFQ DLHAISDSFD ICKFNAFAEG
IEEYIDQYNG MTGRSVGEEE LMEAGERVYN LERYYNNLAG FDGDDDTLPG RFVEGDEDAV
PAGGGIEGEL CELDAMKQEY YDHRGWVDGV VPDEKLHDLG IDMGPGTGVS TDSSAPADD
//
