(data stored in ACNUC7421 zone)

SWISSPROT: C7QJB0_CATAD

ID   C7QJB0_CATAD            Unreviewed;       362 AA.
AC   C7QJB0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   05-JUL-2017, entry version 51.
DE   SubName: Full=Glu/Leu/Phe/Val dehydrogenase dimerisation region {ECO:0000313|EMBL:ACU69252.1};
GN   OrderedLocusNames=Caci_0299 {ECO:0000313|EMBL:ACU69252.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69252.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69252.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|RuleBase:RU004417}.
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DR   EMBL; CP001700; ACU69252.1; -; Genomic_DNA.
DR   ProteinModelPortal; C7QJB0; -.
DR   STRING; 479433.Caci_0299; -.
DR   EnsemblBacteria; ACU69252; ACU69252; Caci_0299.
DR   KEGG; cai:Caci_0299; -.
DR   eggNOG; ENOG4107RDP; Bacteria.
DR   eggNOG; COG0334; LUCA.
DR   HOGENOM; HOG000243800; -.
DR   KO; K00271; -.
DR   OMA; TYVADMD; -.
DR   OrthoDB; POG091H0EKI; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR016211; Glu/Phe/Leu/Val_DH_bac/arc.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR42722:SF1; PTHR42722:SF1; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 2.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000188; Phe_leu_dh; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJB0.
DR   SWISS-2DPAGE; C7QJB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU004417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN      149    358       ELFV_dehydrog. {ECO:0000259|SMART:
FT                                SM00839}.
FT   ACT_SITE     85     85       {ECO:0000256|PIRSR:PIRSR000188-1}.
SQ   SEQUENCE   362 AA;  38750 MW;  EC0BACCFF32090D0 CRC64;
     MSDKPDNDVS EVFASDHEQV VYCRDEETGL KAIIAVHNTL LGPGLGGTRF FPYATEQDAL
     KDVLRLSRGM SYKNALAGLD LGGGKAVIIG DPSEIKTEAL LRAYGRFVQS LNGRYYTACD
     VGTYVQDMDV VAKESRFVTG RSMESGGAGD SSVLTAYGVF QGMRASAEYL WGSPSLAGKR
     VGISGVGKVG RYLIGHLIED GASIVATDPY EGAIQWLRDN YAQVELVSTT EDLIAADIDV
     YAPCALGGAL DDATVAALTA KIVCGAANNQ LAHTGVEKQL EARGILYAPD YLVNSGGVIQ
     VADEIHGFDF ERAKRRASGI FDTTMRIYSL ASEEGVPPSV AADRLAERRM RDVGRLRGVY
     LP
//

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