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Database: UniProt
Entry: A0A0P7ZLD4_9EURY
LinkDB: A0A0P7ZLD4_9EURY
Original site: A0A0P7ZLD4_9EURY 
ID   A0A0P7ZLD4_9EURY        Unreviewed;       365 AA.
AC   A0A0P7ZLD4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:KPQ44934.1};
GN   Name=aor {ECO:0000313|EMBL:KPQ44934.1};
GN   ORFNames=MPEBLZ_00472 {ECO:0000313|EMBL:KPQ44934.1};
OS   Candidatus Methanoperedens sp. BLZ1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX   NCBI_TaxID=1719120 {ECO:0000313|EMBL:KPQ44934.1, ECO:0000313|Proteomes:UP000050360};
RN   [1] {ECO:0000313|EMBL:KPQ44934.1, ECO:0000313|Proteomes:UP000050360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Arshad A., Speth D.R., De Graaf R.M., Op Den Camp H.J., Jetten M.S.,
RA   Welte C.U.;
RT   "A metagenomics-based metabolic model of nitrate-dependent anaerobic
RT   oxidation of methane by Methanoperedens-like archaea.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPQ44934.1}.
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DR   EMBL; LKCM01000040; KPQ44934.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7ZLD4; -.
DR   PATRIC; fig|1719120.3.peg.510; -.
DR   Proteomes; UP000050360; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR   Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR   Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR   InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
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;
FT   DOMAIN          4..202
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   365 AA;  39681 MW;  829D6C2798F5B113 CRC64;
     MHGWTGKNVI IDLTDGKIIE NNSDLNELRS YIGGRGLGVK LYYDLVTADI DPLSPENILI
     FTTGPLTGTR APLSGRHVMV SKSPLTGTIF DSSSGGFFGK ELKFASVDAL IIKGAADEPV
     YISIQDDDIR INNANDLWGK NVRQCTDQLS GKGHVACIGR AGERLVPIAN VMNDYFHACG
     RGGLGAVMGS KKLKAIVVKG TRKTVIADEE RFEKGCKEAS NLIKKGSSGL STYGTSALLN
     LMNYQKILPA GNFRKNEFNN ASMVSGEFIK ENYDIKGHAC YNCTIACKHI IKSGAFEGYE
     VPEYETLWSF GPDNNNSDIG SIIKVNRMCN DYGIDTISAG STIAAYAEIM GEDVKEFTEL
     VKKNR
//
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