GenomeNet

Database: UniProt
Entry: Q5ZHT1
LinkDB: Q5ZHT1
Original site: Q5ZHT1 
ID   ACD11_CHICK             Reviewed;         777 AA.
AC   Q5ZHT1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   16-APR-2014, entry version 66.
DE   RecName: Full=Acyl-CoA dehydrogenase family member 11;
DE            Short=ACAD-11;
DE            EC=1.3.99.-;
GN   Name=ACAD11; ORFNames=RCJMB04_33j3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: May function as oxidoreductase (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
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DR   EMBL; AJ721053; CAG32712.1; -; mRNA.
DR   RefSeq; NP_001006367.1; NM_001006367.1.
DR   UniGene; Gga.8980; -.
DR   ProteinModelPortal; Q5ZHT1; -.
DR   STRING; 9031.ENSGALP00000036827; -.
DR   PaxDb; Q5ZHT1; -.
DR   GeneID; 420689; -.
DR   KEGG; gga:420689; -.
DR   CTD; 84129; -.
DR   eggNOG; COG3173; -.
DR   HOGENOM; HOG000131666; -.
DR   HOVERGEN; HBG057142; -.
DR   InParanoid; Q5ZHT1; -.
DR   KO; K11730; -.
DR   PhylomeDB; Q5ZHT1; -.
DR   NextBio; 20823570; -.
DR   PRO; PR:Q5ZHT1; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom.
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; PF01636; APH; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase; Peroxisome;
KW   Reference proteome.
FT   CHAIN         1    777       Acyl-CoA dehydrogenase family member 11.
FT                                /FTId=PRO_0000254148.
FT   NP_BIND     501    511       FAD (By similarity).
FT   NP_BIND     501    504       FAD (By similarity).
FT   NP_BIND     509    511       FAD (By similarity).
FT   NP_BIND     535    537       FAD (By similarity).
FT   NP_BIND     724    728       FAD; shared with dimeric partner (By
FT                                similarity).
FT   NP_BIND     753    755       FAD (By similarity).
FT   REGION      626    629       Substrate binding (By similarity).
FT   BINDING     511    511       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     537    537       FAD (By similarity).
FT   BINDING     654    654       FAD (By similarity).
FT   BINDING     654    654       FAD; shared with dimeric partner (By
FT                                similarity).
FT   BINDING     724    724       FAD (By similarity).
FT   BINDING     752    752       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     755    755       FAD (By similarity).
SQ   SEQUENCE   777 AA;  87002 MW;  061B17C5BC96AF2E CRC64;
     MAVEPGTSEV RRQHRFDQGS LERYLCRCLP GFPQQPAGAL SVRQYSSGQS NPTFYLQKGG
     QAYVLRKKPH GPLLPNAHKV DREYHVQKAL FSAGFPVPEP LLYCSDVSVI GTEFYVMQHV
     QGRIFRDASL PEVGPAERSA LYLAIETLAQ LHSFDLRSLG LQGYGRGPGY CRRQVSTWKR
     QYDAAAHTDI PAMNELAKWL ANNLPPDDDE EALIHGDFRI DNIIFHPTEA RVLAVLDWEL
     STTGHPLADL AYATQFYFWP TSLNVLGQGS VFNFKGTIEN PSFEELISIY CRCRGISTTI
     PNLNFFLALS YFKMAGISQG VYARYLIGNA SAESSHEFAK MVKPLAEKGL ELSKRLSFSS
     IQHNTSGELF YQSRKGQEVL LKVKQFMKQH VYPAEKEIAE YYAKHGNTEE RWKKPPVLER
     LKEMAKAEGL WNLFLPAVSS LSQLDYALIA EETGKRFFAP EVFNCQAPDT GNMEVLHLYG
     TEEQKKEWLE PLLEGKISSC FCMTEPDVAS SDATNMQCSI ERDGNSYVIN GKKWWSSGAG
     NPNCKVAIVM GKTKNSSASR YKQHSMIIVP MDTPGVRLIR PLSVFGYIDE IHGGHFEVHF
     NDVRVPVSNM ILGEGRGFEI AQGRLGPGRI HHCMRSIGAA ETALEILCQR AAQRETFGKK
     LYHHEVVAHW IAECRLSIEQ ARLLTLKTAS KIDTLGNRKA RKEVAMTKVV VPRAVLKVID
     CAIQVCGGAG VSQDFPLASM FAYIRTLRVA DGPDEVHLST IARWELLDQS KKLTAKI
//
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