ID   D5X9X4_THEPJ            Unreviewed;       630 AA.
AC   D5X9X4;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ADG83107.1};
DE            EC=1.2.7.5 {ECO:0000313|EMBL:ADG83107.1};
GN   OrderedLocusNames=TherJR_2264 {ECO:0000313|EMBL:ADG83107.1};
OS   Thermincola potens (strain JR).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC   Thermincola.
OX   NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG83107.1, ECO:0000313|Proteomes:UP000002377};
RN   [1] {ECO:0000313|EMBL:ADG83107.1, ECO:0000313|Proteomes:UP000002377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JR {ECO:0000313|EMBL:ADG83107.1,
RC   ECO:0000313|Proteomes:UP000002377};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT   "Complete sequence of Thermincola sp. JR.";
RL   Submitted (MAY-2010) 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; CP002028; ADG83107.1; -; Genomic_DNA.
DR   RefSeq; WP_013121107.1; NC_014152.1.
DR   AlphaFoldDB; D5X9X4; -.
DR   STRING; 635013.TherJR_2264; -.
DR   KEGG; tjr:TherJR_2264; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_9; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000002377; 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:ADG83107.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002377}.
FT   DOMAIN          5..208
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   630 AA;  68214 MW;  F5EC2B86E642EBD4 CRC64;
     MPYGYNGKIL CVNLTDGSTR MEEKPESWYR KYLGGRGIGA YYLLKDLPAG TDALAPENIL
     VFAVSVVTGV PFPGNARASV VAKSPLTGGF GEAEAGGNWG PELKFAGFDA VVITGKSEKP
     VYLYLRDGQV EIRDAGNLWG LNTSETEKRI FDDTGDPRVK VACIGPGGEN LVRYACITAG
     RHNVFGRLGL GAVMGSKNLK AVAVSGGKRP ETKEPEKIKE ISRWVAQNFN RPDTCGLFYE
     YGTSGGVAMY NAIGSLPSYN FQGGTIEGAE KLTGEYMKEQ GLMIGKTRCF ACPIACRKIA
     RVENSGELDT KSEVHSPEYE TIAALGSNCG ITDPKVVIKA AEMCDEYGLD TISTGVTISF
     VMECAQKGIL PKDLQGDMPV EFGSAETILR CIEMITYRRG IGDIMAEGTK RMAARIGNGA
     EALAVHGKGE ELALQDPRGG KVGAAIGYAV AHNGGDHIQM EHDFQFSQKG PFLKSFEPLG
     VIEPVPTMDL GIDKVRLFVL NQIVWGLYNM LDICIFVPAP GHVLPLTGLC DLVKCATGWD
     TSLYELMKAG ERGIVMTRIF NLREGFGVQD DVIPRRLTEP LTTGESKGSR VEPEQIQQAV
     KNYYEIMGWD HETGAPSPGK LKELGLDWLI
//