(data stored in SCRATCH zone)

SWISSPROT: C1ARQ2_RHOOB

ID   C1ARQ2_RHOOB            Unreviewed;       382 AA.
AC   C1ARQ2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Glutamate dehydrogenase {ECO:0000256|PIRNR:PIRNR000185};
GN   OrderedLocusNames=ROP_04820 {ECO:0000313|EMBL:BAH48729.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48729.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48729.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48729.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC       {ECO:0000256|PIRNR:PIRNR000185, ECO:0000256|RuleBase:RU004417}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP011115; BAH48729.1; -; Genomic_DNA.
DR   RefSeq; WP_012687736.1; NC_012522.1.
DR   EnsemblBacteria; BAH48729; BAH48729; ROP_04820.
DR   KEGG; rop:ROP_04820; -.
DR   PATRIC; fig|632772.20.peg.535; -.
DR   eggNOG; ENOG4105D82; Bacteria.
DR   eggNOG; COG0334; LUCA.
DR   HOGENOM; HOG000243801; -.
DR   KO; K00261; -.
DR   OMA; TNAWWWW; -.
DR   OrthoDB; 1184827at2; -.
DR   BioCyc; ROPA632772:GH0Q-481-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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; IPR014362; Glu_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PIRSF; PIRSF000185; Glu_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; C1ARQ2.
DR   SWISS-2DPAGE; C1ARQ2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   NAD {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000185-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000185,
KW   ECO:0000256|RuleBase:RU004417, ECO:0000313|EMBL:BAH48729.1}.
FT   DOMAIN      140    374       ELFV_dehydrog. {ECO:0000259|SMART:
FT                                SM00839}.
FT   ACT_SITE     74     74       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000185-1}.
FT   BINDING      38     38       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000185-2}.
FT   BINDING      62     62       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000185-2}.
FT   BINDING     149    149       NAD. {ECO:0000256|PIRSR:PIRSR000185-2}.
FT   SITE        110    110       Important for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000185-3}.
SQ   SEQUENCE   382 AA;  39661 MW;  65B2450C80932765 CRC64;
     MFELIDEWGP EKVVCVSDSR TGMRGVLVID NTARGMGKGG TRMSTTVSVG EVARLARNMT
     WKWAGVDLFY GGAKAGIWAD PTASSKEAVL RAFVRALRNE VPEEYVFGLD VGLTEKDAAI
     MLDEVGGRGG AVGTPHALGG LPYDQLGVTG HGVAESADAA AQTLGLSTGS LSVSIQGFGA
     VGAASAKRLA ELGATAVAVS TSRGGIHNPD GLDVAELLTL REQFGDALVD HYSDAKPLAA
     GEELSVTADI LIPAALQDVI DTDLARTLPA RIVVEGANLP STPEAQAVLF DRGVTVVPDF
     IANAGGVVAA AVAMDARFSG IRPEPAAVFD NISNTLRAST IDTLEASKAQ GRTTHEVART
     TAQERVREAM VLRGRAPRNA AF
//

If you have problems or comments...

PBIL Back to PBIL home page