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Database: UniProt
Entry: F8D5I8_HALXS
LinkDB: F8D5I8_HALXS
Original site: F8D5I8_HALXS 
ID   F8D5I8_HALXS            Unreviewed;       555 AA.
AC   F8D5I8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   OrderedLocusNames=Halxa_4222 {ECO:0000313|EMBL:AEH38824.1};
OS   Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halopiger.
OX   NCBI_TaxID=797210 {ECO:0000313|EMBL:AEH38824.1, ECO:0000313|Proteomes:UP000006794};
RN   [1] {ECO:0000313|EMBL:AEH38824.1, ECO:0000313|Proteomes:UP000006794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18323 / JCM 14033 / SH-6
RC   {ECO:0000313|Proteomes:UP000006794};
RX   PubMed=22675596; DOI=10.4056/sigs.2505605;
RA   Anderson I., Tindall B.J., Rohde M., Lucas S., Han J., Lapidus A.,
RA   Cheng J.F., Goodwin L., Pitluck S., Peters L., Pati A., Mikhailova N.,
RA   Pagani I., Teshima H., Han C., Tapia R., Land M., Woyke T., Klenk H.P.,
RA   Kyrpides N., Ivanova N.;
RT   "Complete genome sequence of Halopiger xanaduensis type strain (SH-6(T)).";
RL   Stand. Genomic Sci. 6:31-42(2012).
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; CP002839; AEH38824.1; -; Genomic_DNA.
DR   RefSeq; WP_013881710.1; NC_015666.1.
DR   AlphaFoldDB; F8D5I8; -.
DR   STRING; 797210.Halxa_4222; -.
DR   GeneID; 10799161; -.
DR   KEGG; hxa:Halxa_4222; -.
DR   eggNOG; arCOG00706; Archaea.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000006794; Chromosome.
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   ECO:0000313|EMBL:AEH38824.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006794}.
FT   DOMAIN          11..206
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
FT   REGION          206..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  59858 MW;  2533B67E5B8AC97C CRC64;
     MLHSRGPLRT VDVGERTARE TSIDDVLERF IGGRAAATVL AHDRIPFDAA PFGPENRLYL
     STGPLQQSRM SFTGRMNMTG LSPLTDGLTS ANAGGYLSRN FVGTGISALE IVGESDELLA
     IHVRDDGATF EPVPELEGVT VPETADYVQE HHNLGPEHCV AIGPAGENRV RFASAMTYDS
     RAFGRGGLGA VLGAKNVKCI TFDGDAEPPV DIPDAPQTEV HRAGARSDDQ RRRQGTTGST
     EFINDHFSLP TRYFADTSFE GAAAIGGEAV AEKKYEKGAC SACAYACKLP TRDEETGLET
     EGPEFETVYA FGSLQGIDDI VDVMRANELC DSLGMDTISA GVTVAAYLAS VDEFGNAELA
     QELTEKIAYR EGIGETLADG LARCHDELGV ADYTVKGMEL PAHDGRVLHG QGLSYAVSNR
     GADHLYASML TLEYGGELDP RGTVGKADRL AREENTAALF DTGIICVFGG DYVTEEYLET
     LFDADYEDLL EVGARTVLLE RHFNNQRGFD REDDTLPYEI PDLEAAITAY YEARGLNEDG
     TVPESALEER IDTAD
//
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