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Database: UniProt
Entry: E8QZY7_ISOPI
LinkDB: E8QZY7_ISOPI
Original site: E8QZY7_ISOPI 
ID   E8QZY7_ISOPI            Unreviewed;       653 AA.
AC   E8QZY7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:ADV64263.1};
GN   OrderedLocusNames=Isop_3707 {ECO:0000313|EMBL:ADV64263.1};
OS   Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Isosphaera.
OX   NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV64263.1, ECO:0000313|Proteomes:UP000008631};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43644;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.;
RT   "The complete sequence of chromosome of Isophaera pallida ATCC 43644.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV64263.1, ECO:0000313|Proteomes:UP000008631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC   {ECO:0000313|Proteomes:UP000008631};
RX   PubMed=21475588; DOI=10.4056/sigs.1533840;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL   Stand. Genomic Sci. 4:63-71(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; CP002353; ADV64263.1; -; Genomic_DNA.
DR   RefSeq; WP_013566551.1; NC_014962.1.
DR   AlphaFoldDB; E8QZY7; -.
DR   STRING; 575540.Isop_3707; -.
DR   KEGG; ipa:Isop_3707; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_11_1_0; -.
DR   InParanoid; E8QZY7; -.
DR   OMA; NAFMGLR; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000008631; 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   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; 2.
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   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF9; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL; 1.
DR   Pfam; PF21343; ACAD9-ACADV_C; 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.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008631}.
FT   DOMAIN          95..200
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          204..304
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          317..459
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   653 AA;  70577 MW;  631BDCB53019806C CRC64;
     MSTAAPERGR AALDSPPSPE PGRVPGSPKD RGPGTSAAPT AEELNAKQIA QAEELLFSGP
     PKHGFVKALY QGRFRAEAIF PYPEEPPAAR AAADQAVDEV RRFLEEHVDP ARIDREADIP
     RSVIEGLGRV GVLGMTAPVE VGGRGLSQSG YCRVMEVIGG HCASTSVFVN AHHSIGIRAL
     LLFGTEEQKS RWLPGLVRGE KLAAFALTEP EAGSDAGNVQ TTAEPIQTEE GPAYQLNGQK
     RYITNGGIAD VLTVMARTPD PKGGESKITA FLVTPDLPGF RVLEERKPKC GIRGTATGAL
     AFNEMIVPAS NVLGPVGKGL RVALTVLDFG RTTFGACCTG VAKVCLKAAV RHASTRRQFG
     KTLGSFELVK KKIAFIAAHT YAMEATTRHA AALIDSGAED YMLETGILKV FATEVLWDIV
     YETLQIHGGQ GYFNDEPYER MMRDARINTI GEGANEVLKG YLIALAGMRD LGKEFEAVFR
     DFTSGSSKFF GGLWGLTKNQ ARLTIQTPHV PVTRVELLPF AKQLAKRVKR FGWAVQKTIV
     TAGGPLTDLP GVVKFGKAAE KAMLGHMGKL MDRQMIQERI ADAVIALYTA SCVLSRLDHE
     LNRGDLTPLN RKAGELFLRM SFRKFDRCLD GLKSNDDPHV VEVADLALAQ FQA
//
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