ID   A9BF59_PETMO            Unreviewed;       604 AA.
AC   A9BF59;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Aldehyde ferredoxin oxidoreductase {ECO:0000313|EMBL:ABX31123.1};
DE            EC=1.2.7.5 {ECO:0000313|EMBL:ABX31123.1};
GN   OrderedLocusNames=Pmob_0381 {ECO:0000313|EMBL:ABX31123.1};
OS   Petrotoga mobilis (strain DSM 10674 / SJ95).
OC   Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC   Petrotoga.
OX   NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31123.1, ECO:0000313|Proteomes:UP000000789};
RN   [1] {ECO:0000313|EMBL:ABX31123.1, ECO:0000313|Proteomes:UP000000789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Noll K., Richardson P.;
RT   "Complete sequence of Petroga mobilis SJ95.";
RL   Submitted (NOV-2007) 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; CP000879; ABX31123.1; -; Genomic_DNA.
DR   RefSeq; WP_012208230.1; NC_010003.1.
DR   AlphaFoldDB; A9BF59; -.
DR   STRING; 403833.Pmob_0381; -.
DR   KEGG; pmo:Pmob_0381; -.
DR   eggNOG; COG2414; Bacteria.
DR   HOGENOM; CLU_020364_1_0_0; -.
DR   OrthoDB; 9763894at2; -.
DR   Proteomes; UP000000789; 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:ABX31123.1}.
FT   DOMAIN          6..208
FT                   /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00790"
SQ   SEQUENCE   604 AA;  65213 MW;  7A7D98185C3361AF CRC64;
     MIKGGFKGKL LRVNLTTKEV KSEPLNEEWA QKYLGGRGYG TRLLLEEIDP KVDPLSEENK
     VIFATGPLDG TLAPSSGRTM VITKGPLNGA IACSNAGGHF GPALKHTGYD MIVVEGKSAE
     PVYIWINKGK VEFRSAKEIW GKLADESDEL IREQTHPLAE TMTIGPAGEK LSPISSVMFN
     GHRASGRTGV GAAVGSKNLK GIAVRGNEDT PVADPEAFMK AVYKARDILS KDAFAGQGAA
     MLGTAMLVNV INGVGGFPTR NAQDAYFPEA NKISGETLRE KNLIRNEGCA ECPIACGRVT
     VVKSGPYKGT IGGGPEYESV WSFGAMCGVS DLDAVISANH LCDKYGIDTI AMGSTVACAM
     ELYEKGYMPK EDAPFELRFG SAEAMLKAVE LACKQEGNFG KLLAQGSYRL AEHYGHPELS
     MSAKKQEFPA YDPRAIKGMG LEYATSNRGA CHVRGYGTAV EVLGDADQYA YEGKAAIIKT
     LQDLTGALDS SGICLFTTFG LSANELAEMV STATGFSIDA QEFMKIGERI WNIEKLFNLK
     AGFTRQDDTL PPRILNEPIK TGPSKGQVED LEKMLDEYYQ LRGWDKDSVP TEEKLKELEV
     QISK
//