GenomeNet

Database: UniProt
Entry: A0A0F7PB88_9EURY
LinkDB: A0A0F7PB88_9EURY
Original site: A0A0F7PB88_9EURY 
ID   A0A0F7PB88_9EURY        Unreviewed;       641 AA.
AC   A0A0F7PB88;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE            EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN   ORFNames=HLASF_1957 {ECO:0000313|EMBL:AKH98426.1};
OS   Halanaeroarchaeum sulfurireducens.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halanaeroarchaeum.
OX   NCBI_TaxID=1604004 {ECO:0000313|EMBL:AKH98426.1, ECO:0000313|Proteomes:UP000069906};
RN   [1] {ECO:0000313|EMBL:AKH98426.1, ECO:0000313|Proteomes:UP000069906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSR2 {ECO:0000313|EMBL:AKH98426.1,
RC   ECO:0000313|Proteomes:UP000069906};
RX   PubMed=25978546;
RA   Sorokin D.Y., Kublanov I.V., Gavrilov S.N., Rojo D., Roman P.,
RA   Golyshin P.N., Slepak V.Z., Smedile F., Ferrer M., Messina E., La Cono V.,
RA   Yakimov M.M.;
RT   "Elemental sulfur and acetate can support life of a novel strictly
RT   anaerobic haloarchaeon.";
RL   ISME J. 0:0-0(2015).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP008874; AKH98426.1; -; Genomic_DNA.
DR   RefSeq; WP_050049090.1; NZ_CP008874.1.
DR   AlphaFoldDB; A0A0F7PB88; -.
DR   GeneID; 25160108; -.
DR   KEGG; hsu:HLASF_1957; -.
DR   PATRIC; fig|1604004.4.peg.2052; -.
DR   HOGENOM; CLU_020364_1_0_2; -.
DR   OrthoDB; 30771at2157; -.
DR   Proteomes; UP000069906; 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: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:AKH98426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069906}.
FT   DOMAIN          7..212
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
FT   REGION          269..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  68786 MW;  7300306A42337023 CRC64;
     MTDIGGFNDR VARIDLSSGA TEYEEIDDED AKKYVGGRGL GVKYVFENGP DVDPLGPDNL
     LAFMTGPLTG TQATMSGRIA VVTKSPLTNT VTDSHHGGWS GARLKWSGFD GLLFEGQADD
     PVYAYVEDGE VELRDASHLW GMTTHEARET IEEELDGAYG KNLSFMGIGP GGENLVRFGA
     IINEDDRASG RGGTGAVMGS KNLKAVVVKS GTDMPQPADE ETFEDGAGQA TGAIMESDVT
     APNEGGLSVY GTNVLMNLTE EMDGLPTRNG QFTSTSAEAE ADPSEPNIDA ENTSGEWVRE
     NILVDEPTCH SCPVACKKEV EVQTTVGGAD RSVRMESLEY EPAFTMGSNA MNDDAELTAV
     LIDRCNKLGI DAIESGNMLS MAMEMSEKGH IEEDIEWGDR DAMYEVLRRI AEREDDLGDA
     LAEGAAGAAE RFDAHDSRLD VKNQTIPAYD PRAMKGMAIG YATSNRGACH LRAYTPAAEI
     LGIPQKVDPA DPEGKGDLAI TFQDLHAVSD SFDICKFSAF AEGIEEYSKQ FNGMTGLDLS
     EDELVEAGKR IYTLERYYNN LVGFEGEDDS LPGRFVEGHE DAIPGQGAAE GQLAELDQLK
     DEYYEGRQWV DGVVPDERLD ELDIEVGPGT GVSGGGAAAD D
//
DBGET integrated database retrieval system