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Database: UniProt
Entry: A0A1M4XG70_9FIRM
LinkDB: A0A1M4XG70_9FIRM
Original site: A0A1M4XG70_9FIRM 
ID   A0A1M4XG70_9FIRM        Unreviewed;       585 AA.
AC   A0A1M4XG70;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Aldehyde:ferredoxin oxidoreductase {ECO:0000313|EMBL:SHE92627.1};
GN   ORFNames=SAMN02745218_01089 {ECO:0000313|EMBL:SHE92627.1};
OS   Desulfofundulus australicus DSM 11792.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofundulus.
OX   NCBI_TaxID=1121425 {ECO:0000313|EMBL:SHE92627.1, ECO:0000313|Proteomes:UP000184196};
RN   [1] {ECO:0000313|EMBL:SHE92627.1, ECO:0000313|Proteomes:UP000184196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11792 {ECO:0000313|EMBL:SHE92627.1,
RC   ECO:0000313|Proteomes:UP000184196};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FQUW01000011; SHE92627.1; -; Genomic_DNA.
DR   RefSeq; WP_073163839.1; NZ_FQUW01000011.1.
DR   AlphaFoldDB; A0A1M4XG70; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000184196; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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}.
FT   DOMAIN          4..207
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   585 AA;  64015 MW;  8FCAA3A2840B9A6F CRC64;
     MYGFYGRLLR LNLSDRSFAV EELPESVYRD YLGGKGLGTY LLLRELEPGI DPLSPANKLI
     IAIGPATGTV LPGSSRYGVF SKSPLTGLYA ESYAGGRVAP AIRRTGYDAV IIEGAADAPL
     YVEISDKNVL FHDASHLWGK DTYATEDAVL AEVGQKGAGA MVIGPAGENL VRFACIENNY
     WRSAGRTGMG AVMGSKKLKA LVFHGEARCE MADPALLQEA ARRIREKGRD NPGVKAYQTY
     GTTVMVGSMN AARAFPARYW TMAVDPGWEN ISGDTLRKKF EVQPRACPNC FMACGKLTTI
     KEGKRAGLTL EGPEYETIYS FGGLCGINSL EEIIYLNDLC DRLGMDTITT GNLVALMMEA
     GKRGRVKGYP GYGDAEGAAR LVEDMAYSRG SGELLARGIK HVAAELGLED LAVHVKGLEP
     AGYDPRVLKG MGLAYATSPR GACHLRATFY KPELSGMIDP STTEGKAALF IEFENRLTVF
     NTMIFCVFFR DLIQWDDLVA MIRGSTGWEY TREELACLAG RIVTATRLFN TREGATRADD
     MLPPRFFDEP VNDGRNVITR QELDVMLDDY YRLRGWDQNG VPPGN
//
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