ID A0A1F4E2Q5_9PROT Unreviewed; 373 AA.
AC A0A1F4E2Q5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Pimeloyl-CoA dehydrogenase small subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3F77_18610 {ECO:0000313|EMBL:OGA54996.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_12_FULL_67_28.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797503 {ECO:0000313|EMBL:OGA54996.1, ECO:0000313|Proteomes:UP000177406};
RN [1] {ECO:0000313|EMBL:OGA54996.1, ECO:0000313|Proteomes:UP000177406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGA54996.1}.
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DR EMBL; MERO01000246; OGA54996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4E2Q5; -.
DR STRING; 1797503.A3F77_18610; -.
DR Proteomes; UP000177406; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd00567; ACAD; 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 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 PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43884:SF44; BLR1022 PROTEIN; 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 SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-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};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125}.
FT DOMAIN 6..117
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 121..193
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 224..362
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 373 AA; 40231 MW; 7F7B8D419A192F6E CRC64;
MNFDYNEEQQ LLADSVRRFL AKDYEFDKRR KIVASSEGWS AETWATLAEM GVTGLPLPAQ
FGGFGGGAVD LMGVMEAFGE ALVVEPYLAT VLAARLVARA GSEAQKKAIL PQVVEGKLRL
AFAHTEKGAR YNLAQVRTEA TPADGGWALN GEKVVVLGAP LAEKIVVSAR SAKGMSLFLV
DRGALKLRPY RTLDEMRAGD VMLASVKVGA DALLGRDGEA LALIEEATDF ATALVCAEAV
GAMKFACDTT LEYLKTRKQF GVPIGTFQAL QHRMVDMYIA YEQAKSMACV ACSRADHAAD
ARERQLAVSA AKIKISDNCR HISQESVQLH GGMGMAEELK VSHSFRRLTM IAQQFGDAEH
HLARFAALDA SGA
//
