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Database: UniProt
Entry: E7RR23_9BACT
LinkDB: E7RR23_9BACT
Original site: E7RR23_9BACT 
ID   E7RR23_9BACT            Unreviewed;       575 AA.
AC   E7RR23;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Acyl-CoA dehydrogenase, C-terminal domain protein {ECO:0000313|EMBL:EFZ36711.1};
GN   Name=acd {ECO:0000313|EMBL:EFZ36711.1};
GN   ORFNames=HMPREF0663_11624 {ECO:0000313|EMBL:EFZ36711.1};
OS   Hoylesella oralis ATCC 33269.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=873533 {ECO:0000313|EMBL:EFZ36711.1, ECO:0000313|Proteomes:UP000005580};
RN   [1] {ECO:0000313|EMBL:EFZ36711.1, ECO:0000313|Proteomes:UP000005580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33269 {ECO:0000313|EMBL:EFZ36711.1,
RC   ECO:0000313|Proteomes:UP000005580};
RA   Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA   Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA   Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA   Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA   Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA   Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA   Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA   Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA   Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA   Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA   Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA   Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA   Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA   Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) 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:EFZ36711.1}.
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DR   EMBL; AEPE02000005; EFZ36711.1; -; Genomic_DNA.
DR   RefSeq; WP_004369779.1; NZ_GL833119.1.
DR   AlphaFoldDB; E7RR23; -.
DR   STRING; 28134.SAMN05444288_1272; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_12_2_10; -.
DR   Proteomes; UP000005580; 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   Gene3D; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR   InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 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; PF12186; AcylCoA_dehyd_C; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF158494; PG0775 C-terminal 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005580}.
FT   DOMAIN          91..169
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          173..268
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          283..444
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          452..563
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12186"
SQ   SEQUENCE   575 AA;  65083 MW;  7DC1D36BFFA7A3EE CRC64;
     MSNYYTDHPE IEFHLNHPLM KRIVDLKERN YADKDKFEDA PVSYEDAIEN YKRILDIAGD
     IAANIVEPNS ESVDLEGPHL ENNRMIYASK TFENLDATRK AGLWGISMPR RYGGLNLPNT
     TFSMLSEVIS AADSGFQNIW SLQSCIDTLY EFGNEEQRQK YIPRICAGET MSMDLTEPDA
     GSDLQRVMLK ATFDEKENCW RLNGVKRFIT NGDSDIHLVL ARSEEGTHDG RGLSMFIYDK
     RNGGVDVRHI ENKLGIHGSP TCELVYKNAK AELCGNTRLG LIKYVMALMN GARLGIAAQS
     VGVEQEAYNE ALAYAKERAQ FGQKIINFPA VYDMLSRMKA KLDAGRSLLY QTARYVDIYK
     ALEDIQRDTK LIAEERDELK KYTRLADAFT PLAKGMNSEY ASQAAYDAIS IHGGSGFIME
     YKSQRLYRDA RIFSIYEGTT QLQVVAAIRY ITNGTYLGII REMLGNEVVE SLTPLQTRVA
     KLAEQYEEVL NEVKEEGNQE KQDFVARRLF NMTADIIMSL LILDDATHSP ELFAKSANVF
     VRHAEEEVTG HYAYIKNLCA EDLVNFRTAE VETAE
//
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