ID B0VEX1_CLOAI Unreviewed; 710 AA.
AC B0VEX1;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Tungsten-containing aldehyde ferredoxin oxidoreductase, alpha chain {ECO:0000313|EMBL:CAO80592.1};
DE EC=1.2.7.5 {ECO:0000313|EMBL:CAO80592.1};
GN Name=aorA {ECO:0000313|EMBL:CAO80592.1};
GN OrderedLocusNames=CLOAM0709 {ECO:0000313|EMBL:CAO80592.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO80592.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO80592.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
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; CU466930; CAO80592.1; -; Genomic_DNA.
DR RefSeq; WP_015424451.1; NC_020449.1.
DR AlphaFoldDB; B0VEX1; -.
DR STRING; 459349.CLOAM0709; -.
DR KEGG; caci:CLOAM0709; -.
DR eggNOG; COG2414; Bacteria.
DR HOGENOM; CLU_020364_1_0_0; -.
DR OrthoDB; 9763894at2; -.
DR Proteomes; UP000002019; 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:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE: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:CAO80592.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002019}.
FT DOMAIN 20..238
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 710 AA; 79965 MW; A16462C7FBC1FE5D CRC64;
MNRKLISEFK YDLAPVIRGY NKRSLYINLS TNEIKQKPVT ELMIDKFVGG KGFDLYLMWH
SVQDDTKWDS PENEICISFG PLCGNTSYPG SGKSIVTTIS PLTGIPVDCN VGGHFGPYAK
FSGWDAIELQ GIANEEVIIY IDGDKGIVQI LSAPDEEINS HILAEELIKE FADGPDKYQF
VSVVSSGKAA DNVLITCLNF SFWDKRRKVA RLKQAGRGGT GSVFRHKKIK ALVVKYSGLK
VDSNNPEDAE TLRMTGLKLH KEIEEGDATQ NRMRQVGTAH LMEIMNDYDL LPIRNFKYGQ
SPEAEGLHSR EFKNLFTQGM PDGCWYGCSL SCCKGVDNFE PRTGPYKGQK VCVDGPEYET
AAGCGSNIGV FNARDVVEIN FYCDTYGVDT ISFGTSTAFA MECYENGILN KERTGGLELT
WGNADAALEL LHQMAKGEGF GVIVGQGVRR MKQIFAEKYG ADPNFLQDIG MEAKGLEYSQ
YMSKESLAQQ GGYTLALKGP QHDEAWLIFM DMVNNQIPTF KDKAEALHYF PMFRTWFGLQ
GLCKLPWNDI EPANNAETDE PAKVPEHVQN YVDIYKAITG KPLDKVSLIE QSERVYNFQK
VFCLRMGKGR RIDDVPPYRA VGPVTEEEYL SRQERYDQQL KEKIGVDPEG KSTAEKMDIL
RKYREDQYQQ LIDAVYERKG WTKEGVPKIE HLQKIGMDLP EVVEVVKRFL
//
