ID A6M3I2_CLOB8 Unreviewed; 634 AA.
AC A6M3I2;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ABR37162.1};
GN OrderedLocusNames=Cbei_5056 {ECO:0000313|EMBL:ABR37162.1};
OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS acetobutylicum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=290402 {ECO:0000313|EMBL:ABR37162.1, ECO:0000313|Proteomes:UP000000565};
RN [1] {ECO:0000313|EMBL:ABR37162.1, ECO:0000313|Proteomes:UP000000565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA Blaschek H., Richardson P.;
RT "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR37162.1, ECO:0000313|Proteomes:UP000000565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX PubMed=21962126; DOI=10.1186/1471-2164-12-479;
RA Wang Y., Li X., Mao Y., Blaschek H.P.;
RT "Single-nucleotide resolution analysis of the transcriptome structure of
RT Clostridium beijerinckii NCIMB 8052 using RNA-Seq.";
RL BMC Genomics 12:479-479(2011).
RN [3] {ECO:0000313|EMBL:ABR37162.1, ECO:0000313|Proteomes:UP000000565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51743 / NCIMB 8052 {ECO:0000313|Proteomes:UP000000565};
RX PubMed=22433311; DOI=10.1186/1471-2164-13-102;
RA Wang Y., Li X., Mao Y., Blaschek H.P.;
RT "Genome-wide dynamic transcriptional profiling in clostridium beijerinckii
RT NCIMB 8052 using single-nucleotide resolution RNA-Seq.";
RL BMC Genomics 13:102-102(2012).
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; CP000721; ABR37162.1; -; Genomic_DNA.
DR AlphaFoldDB; A6M3I2; -.
DR KEGG; cbe:Cbei_5056; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_021577_0_0_9; -.
DR Proteomes; UP000000565; 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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 583..634
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
SQ SEQUENCE 634 AA; 68929 MW; 55BD21CFB86D882F CRC64;
MFFKTTEQHE NLRTKIREFA EEEVKPIAFM LDQENKFPSE VVQRLADMGV MGIPYSKEYG
GAGLDVISYA IAVEELSRVD GGTGVILSAH TSLGTYPIAA FGNEEQKQKY LVPLAKGEKL
GAFGLTEENA GSDAGGTETT AVLEGDYYIL NGEKIFITNG GEADIYIVFA VTTPNIGTRG
ISAFIVEKGS EGFSFGKHYD KMGIRSSATA ELIFNDVKVP KENLLGKEGD GFKIAMSTLD
GGRIGIAAQA LGIAQGAYEN ALEYSKERVQ FGKPICQQQI IAFKLADMAT KLRAARFLIY
SAAELKGNHE HYSMEAAMAK QYASDVCLEI VNDALQIFGG SGYLKGMEVE RAYRDAKICT
IYEGTNEIQR VVIAANIIGK MPKTESVAKT SREPATGYRK KVIYKDGTPE ERVNSLVEAL
KKDGYDFSVG IPIDTPISKA ERVVSVGQGI GEKENMNLIE KLAVQAGAAI GSSRPVAETL
KYVPIDRYVG MSGQKFKGNL YIACGISGAG QHLKGIKDAS TIVAININPN AKIFKNSDYG
IVGDLMEILP LLIEALDNGE PKKEAPPMKK MKRVIPKKVT PTWKHYVCNG CGYEYDPGVG
DLEGEVNPGT LFENLPEEWT CPACGEEKDM FIEV
//
