ID F7V985_CLOSS Unreviewed; 642 AA.
AC F7V985;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Rubredoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50903};
GN OrderedLocusNames=CXIVA_07280 {ECO:0000313|EMBL:BAK46695.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK46695.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR EMBL; AP012212; BAK46695.1; -; Genomic_DNA.
DR AlphaFoldDB; F7V985; -.
DR STRING; 1042156.CXIVA_07280; -.
DR KEGG; cls:CXIVA_07280; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_021577_0_0_9; -.
DR OrthoDB; 9802447at2; -.
DR Proteomes; UP000008937; Chromosome.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00730; rubredoxin; 1.
DR CDD; cd01158; SCAD_SBCAD; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR014731; ETF_asu_C.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR024935; Rubredoxin_dom.
DR InterPro; IPR018527; Rubredoxin_Fe_BS.
DR PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF25; ACYL-COA DEHYDROGENASE; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF00766; ETF_alpha; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00202; RUBREDOXIN; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000008937};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 586..637
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 642 AA; 68703 MW; D187FFF58CDED1E5 CRC64;
MLFQTSKEHE ALRAEIRAFA EKEIAPIAFR LDKENEFPTE QVKQMAEHGW MGLPYPKEYG
GAGADVISYA IAVEELARVD GGTGVILSAH TSLGTYPIAA YGTEEQKKKY LVPLASGQKL
GAFGLTEENA GSDAGGTETT AIDKGDHYLL NGGKIFITNA PKADIYVVFA VTTPDIGTRG
ISAFIVEKGW KGFEFGDHYD KLGIRSSSTA ELIFNNVKVP KENLLGKEGQ GFKIAMSTLD
GGRIGIAAQA LGIAQGAYDK ALEYAKERVQ FGEPIGVHQG ISFKLADMAT KLQAARFLIY
SAAELKENHE RYGMEAAMAK MYASDAAVEI TNDALQIFGG SGYLKGMEVE RAFRDAKITT
IYEGTNEIQR VVIAANLLGK ISKNTGGGSR SVMKKPAPVT GIRKNRIFTE GEAADKVNDL
VAALKSDGYD FSVGIPADTP IPQAERVVSA GKGIGDKANM KLIEDLAHAA GAAIGSSRPV
AETLQYVPLN RYVGMSGQKF TGNLYIACGI SGAKQHLKGI KDASTIVAIN KNGNAPIFKN
CDYGIVGDVN EILPLLTKAL GTGKKAPAGK MIKMKRPLPP KPEPIGPRYI CSGCAYEYIP
ELGDEEADIA PGTLFKDLPA DWVCPECAED KDHFIEAGIR GL
//
