ID A0A137SXF7_9FIRM Unreviewed; 693 AA.
AC A0A137SXF7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Rubredoxin {ECO:0000313|EMBL:KXO17089.1};
GN ORFNames=HMPREF3189_00056 {ECO:0000313|EMBL:KXO17089.1};
OS Clostridiales bacterium KA00134.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1588750 {ECO:0000313|EMBL:KXO17089.1, ECO:0000313|Proteomes:UP000070500};
RN [1] {ECO:0000313|EMBL:KXO17089.1, ECO:0000313|Proteomes:UP000070500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00134 {ECO:0000313|EMBL:KXO17089.1,
RC ECO:0000313|Proteomes:UP000070500};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXO17089.1}.
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DR EMBL; LTAF01000002; KXO17089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137SXF7; -.
DR STRING; 1588750.HMPREF3189_00056; -.
DR PATRIC; fig|1588750.3.peg.56; -.
DR Proteomes; UP000070500; Unassembled WGS sequence.
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 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; 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:UP000070500};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 635..686
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 74780 MW; 47DA7820B10D9BE6 CRC64;
MSFFKKKKSS GKKKAFEEKK ETVTEKVEKV SATKEVETES KSKEGGGKSM YRPNEAQEAL
RRKVREFAEA EVKPIAFSLD QNNEYPDEIV AKMAELGIMG LPYEKKYGGS EEGAVAYAIA
VEELSRVDGG VGVILSAHTS LGSYPIEAFG NEAQKEKYLV PLAKGEKVGA FGLTEPEAGS
DASGTQTTAE LDGDYYILNG NKIFITNAPK ADTYVVFAVT TPGIGTHGIS AFIVEKGWEG
FTFGDHYDKL GIRSSTTAEL IFNNVKVPKE NLLGQEGQGF RIAMQTLDGG RIGIAAQALG
IAQGAYEAAL AYAKERIQFG RPIAQQQAIS FKLADMATKL RAARLMIYSA AEMKQNHENF
GMEAAMAKMY ASDVAMEITN DALQIHGGNG YLKGMEVERH YRDAKITQIY EGTNEIQRVV
IASNIIGRLP KRGGSKGGPA PAAKQGPITG ERKREIIKAD TAQEAVDKLV ASLKKDGYDF
SVGIDIDTPI SDAERVVSVG KGIGSAENLE KAKVLAHAAG AALGSSRPVA ENMKLLPLER
YVGMSGQKFR GNLYIALGIS GASQHLKGIK DASTIVAINK NAGAPIFKNA DYGIVGDMNE
IMPLLAKALG TGEKKPAPPM KKVRRSKPRK LAPNYDVHVC VGCGYEYDPN VGDPEAEISP
GTMFEKLPED WVCPNCQEEK SGFIVENYPA DRK
//
