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Database: UniProt
Entry: F5YRG3_TREPZ
LinkDB: F5YRG3_TREPZ
Original site: F5YRG3_TREPZ 
ID   F5YRG3_TREPZ            Unreviewed;       578 AA.
AC   F5YRG3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Acyl-CoA dehydrogenase family protein {ECO:0000313|EMBL:AEF85362.1};
GN   Name=acd {ECO:0000313|EMBL:AEF85362.1};
GN   OrderedLocusNames=TREPR_1267 {ECO:0000313|EMBL:AEF85362.1};
OS   Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF85362.1, ECO:0000313|Proteomes:UP000009223};
RN   [1] {ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA   Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA   Paulsen I.T.;
RT   "Complete sequence of Treponema primitia strain ZAS-2.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEF85362.1, ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RX   PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA   Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT   "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT   spirochete species in co-culture.";
RL   ISME J. 5:1133-1142(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; CP001843; AEF85362.1; -; Genomic_DNA.
DR   RefSeq; WP_015708811.1; NC_015578.1.
DR   AlphaFoldDB; F5YRG3; -.
DR   STRING; 545694.TREPR_1267; -.
DR   KEGG; tpi:TREPR_1267; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_12_2_12; -.
DR   OMA; FPAVYDM; -.
DR   OrthoDB; 335553at2; -.
DR   Proteomes; UP000009223; 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; 1.20.120.470; 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; 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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 2.
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.
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:UP000009223}.
FT   DOMAIN          94..171
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          175..269
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          284..359
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          389..445
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          458..559
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12186"
SQ   SEQUENCE   578 AA;  64149 MW;  BE6061CD19C58724 CRC64;
     MENFLNDNED ILFHLEHMDL DRIIRFKEEE FTQAQQYSYA PKDAADAKDS YKRVLSIIGE
     ICGEFIAPNA PKVDEEGPVL DLATNQVTLN PATQKAMDMF AQADLLGFCV PRQYGGLNMP
     STILCIAAEI LSRADGSSLN FGLQQDIAGT INKFASEEQK KAVLPKLCSG EWDSSMILTE
     PDAGSDLQAV NLKAVQGEDG KWYLSGVKRF ITNGCGTIGL VLARSEEKGK GARGLSFFLY
     KRDEKMIIRR LEHKLGIHGS PTCELQFNKA PSELVGERQR GLTKYTMWLM NNARLGIAAQ
     AVGIAEAAYR EADLYAAKRI QFDAPVRSLP PVFEMLTEMK VAVEAGRSLL YETARFVDLK
     EALEDYSEAH PDQKGDIVDD KKKYAKLAGF FTPMVKAYAT EMANKVAYDA IQIHGGTGYM
     KEFNAERHYR DARITNIYEG TTQLQVVAAI GPVTSGIAQS ILDEYDQADY PNAGELLAKV
     RASRKIFDET LVYVKAYKGE GHEQFLSYHS RRLVEMATDL VISYLLLRDG VHSERKLKVA
     AIFIAKMPSR IEASRSFITG DDATLLQDYA AVIGQGAV
//
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