ID C5BKC0_TERTT Unreviewed; 1286 AA.
AC C5BKC0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ACR12194.1};
GN OrderedLocusNames=TERTU_2381 {ECO:0000313|EMBL:ACR12194.1};
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629 {ECO:0000313|EMBL:ACR12194.1, ECO:0000313|Proteomes:UP000009080};
RN [1] {ECO:0000313|EMBL:ACR12194.1, ECO:0000313|Proteomes:UP000009080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901 {ECO:0000313|Proteomes:UP000009080};
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347}.
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DR EMBL; CP001614; ACR12194.1; -; Genomic_DNA.
DR RefSeq; WP_015818306.1; NC_012997.1.
DR STRING; 377629.TERTU_2381; -.
DR KEGG; ttu:TERTU_2381; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_002737_0_0_6; -.
DR OrthoDB; 5296889at2; -.
DR Proteomes; UP000009080; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR CDD; cd00567; ACAD; 1.
DR CDD; cd05931; FAAL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR036736; ACP-like_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 InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR22754:SF32; DISCO-INTERACTING PROTEIN 2; 1.
DR PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 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; PF00501; AMP-binding; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1172..1249
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1286 AA; 141549 MW; 5CADE0D5301F2497 CRC64;
MGYEVTFSDR FQEFDSLVGL GRIRASQQKD KIAYSILKYG SGVDDQLTYE QLDIRARALA
ANLQAMKISG RNALLLFPAG LDFVVAFMGC LYAGVAAVPT PMPGRKDKDW IKTGVIAQDA
DVAAVLTVAA QADYVRESMN QDSFLKDVPC VEADVVDEAL SEQWVDPGLA QDDLAFLQYT
SGSTGTPKGV MVTHGNLLHN EEMMRKAYRH TEDTVYVSWL PLFHDMGLIG NVLHTLYLGG
RCYLMTPVAF LQQPLRWLQA ISDYRASTSF APNFAYELCL RRITEEQRDQ LDLSCWTLAL
NGAEPVRADT LERFAEFFGP CGFKWESHYP AYGLAEATLF VSGTGRDEEP FISQVDSQQL
QNHKIVYSDD SKGSQRLVSS GLTNTVQDVV IVNPDNFQRC SADEVGEVWI KGGSVAKGYW
KKAEQTEETF NARIAEDGDG PYLRTGDLGF VSDGRLFITG RLKDVVIVNG ANFYPQDIEL
AVQDNQSVLR HGYGAVFGID QDGSEQVVVV QEVERTQIKK IDHEQVFRNI QQTVVQEFQI
QVAAIVLIKP MTLPLTSSGK IQRRGTRKQF YENDLAEIAC WFGSESLRRE VKGEAVVETA
KPTDLLGSAA ESSVKTEAKI HWLRQYAETR INSALIDERR CVPPYIVMDF ASQGLLGMCV
PEQYAGQAMT VSDSLRVIEQ LAAIDANLAA MVSVHHVLGT RPILNYGSQL TKDVFLPKIA
EGRILGALAI TEPGAGSNPH AISATARPAP QGGWLITGEK CWIGNGSWSG VINTFVQVKD
EQGNPKGLTA FAIEQGRSGM WMGEEAPTMG MRGMVQNRIH FKDVHVTESD MLGRVGQGME
IAQDAMMHGR LVIAAMSLGG LKRAAQLMTR YAQRRDVASG KLFESSVSIQ RLSEMHATIA
AIQAMVRSLG ELIDQGVEIP SEIYAACKTS APEFLWKGVD QLMQMLGGRG YTENNAVPQL
MRDLRLFRIF EGPTEALNVF IGARVINGGE QILSFIKNTL QSSDVATDVA SMASEMLHLA
TASGERIGLN SFQVNQRAHT FVGDLTTLHI VKAFVEFQNQ RCPDKSLQQA IAWLNKCLEI
KHAEVVASTG GSQVWMSAAQ LEQAADDLLH DIGDIQQHAA GMERATDTLL LREGEPVKAP
AAVTPPDLPA TPQEPCAAPE AETVVIANIA TSEEEELEAW MINWLSKRIR VSSSELSAQS
TFVDVGLDSV SSVEFSFELE RWLGFEVDST VVWQYPSISV LTQFLLNEKR TKEAEQQEAE
IHSNQPENLS TLSDDQVAAA LACELE
//
