ID Q4DD33_TRYCC Unreviewed; 477 AA.
AC Q4DD33;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 06-MAR-2013, entry version 53.
DE RecName: Full=Dihydrolipoyl dehydrogenase;
DE EC=1.8.1.4;
GN ORFNames=Tc00.1047053511025.110;
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
OC Schizotrypanum.
OX NCBI_TaxID=353153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener;
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M.A., Myler P.J., Bartholomeu D.C., Nilsson D.,
RA Aggarwal G., Tran A.-N., Ghedin E., Worthey E.A., Delcher A.L.,
RA Blandin G., Westenberger S.J., Caler E., Cerqueira G.C., Branche C.,
RA Haas B., Anapuma A., Arner E., Aslund L., Attipoe P., Bontempi E.,
RA Bringaud F., Burton P., Cadag E., Campbell D.A., Carrington M.,
RA Crabtree J., Darban H., da Silveira J.F., de Jong P., Edwards K.,
RA Englund P.T., Fazelina G., Feldblyum T., Ferella M., Frasch A.C.,
RA Gull K., Horn D., Hou L., Huang Y., Kindlund E., Klingbeil M.,
RA Kluge S., Koo H., Lacerda D., Levin M.J., Lorenzi H., Louie T.,
RA Machado C.R., McCulloch R., McKenna A., Mizuno Y., Mottram J.C.,
RA Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M., Pentony M.,
RA Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J.,
RA Simpson A.J., Sisk E., Tammi M.T., Tarleton R., Teixeira S.,
RA Van Aken S., Vogt C., Ward P.N., Wickstead B., Wortman J., White O.,
RA Fraser C.M., Stuart K.D., Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- CATALYTIC ACTIVITY: Protein N(6)-(dihydrolipoyl)lysine + NAD(+) =
CC protein N(6)-(lipoyl)lysine + NADH.
CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond
CC (By similarity).
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family.
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DR EMBL; AAHK01000630; EAN90443.1; -; Genomic_DNA.
DR RefSeq; XP_812294.1; XM_807201.1.
DR ProteinModelPortal; Q4DD33; -.
DR SMR; Q4DD33; 10-476.
DR GeneID; 3543432; -.
DR KEGG; tcr:511025.110; -.
DR KO; K00382; -.
DR ProtClustDB; CLSZ2429541; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR PANTHER; PTHR22912:SF20; PTHR22912:SF20; 1.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
DR TIGRFAMs; TIGR01350; lipoamide_DH; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Redox-active center.
SQ SEQUENCE 477 AA; 50588 MW; 53D5389EE290B291 CRC64;
MFRRCAVKLN PYDVVVIGGG PGGYVASIKA AQLGMKTACV EKRGTLGGTC LNVGCIPSKA
LLHATHLYHD AHANFARYGL MGGEGVTMDS AKMQQQKERA VKGLTGGVEY LFKKNKVTYY
KGEGSFETAH SIRVNGLDGK QEMFETKKTI IATGSEPTEL PFLPFDEKVV LSSTGALALP
RVPKTMVVIG GGVIGLELGS VWARLGAEVT VVEFAPRCAP TLDEDVTNAL VGALAKNEKM
KFMTSTKVVG GTNNGDSVSL EVEGKNGKRE TLTCEALLVS VGRRPFTGGL GLDKINVAKN
ERGFVKIGDH FETSIPDVYA IGDVVDKGPM LAHKAEDEGV ACAEILAGKP GHVNYGVIPA
VIYTMPEVAS VGKSEEELKK EGVAYKVGKF PFNANSRAKA VSTEDGFVKV LVDKATDRIL
GVHIVCTTAG ELIGEACLAM EYGASSEDVG RTCHAHPTMS EALKEACMAC FAKTINF
//
