(data stored in ACNUC7421 zone)

SWISSPROT: C1AR43_RHOOB

ID   C1AR43_RHOOB            Unreviewed;       487 AA.
AC   C1AR43;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   30-AUG-2017, entry version 53.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   OrderedLocusNames=ROP_02730 {ECO:0000313|EMBL:BAH48520.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48520.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48520.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48520.1,
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 glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; AP011115; BAH48520.1; -; Genomic_DNA.
DR   RefSeq; WP_012687527.1; NC_012522.1.
DR   STRING; 632772.ROP_02730; -.
DR   EnsemblBacteria; BAH48520; BAH48520; ROP_02730.
DR   KEGG; rop:ROP_02730; -.
DR   PATRIC; fig|632772.20.peg.313; -.
DR   eggNOG; ENOG4105C17; Bacteria.
DR   eggNOG; COG0057; LUCA.
DR   HOGENOM; HOG000071677; -.
DR   KO; K00134; -.
DR   OMA; SDLWYDK; -.
DR   OrthoDB; POG091H0F0C; -.
DR   BioCyc; ROPA632772:GH0Q-272-MONOMER; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1AR43.
DR   SWISS-2DPAGE; C1AR43.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361160,
KW   ECO:0000313|EMBL:BAH48520.1}.
FT   DOMAIN      127    287       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
SQ   SEQUENCE   487 AA;  52682 MW;  5FCE30EF9769A452 CRC64;
     MSTAELTQWN SEEALAEAMI PIIGGLHRRH SVTILLHSRS LVNKSVIKIL RTHRFARQIR
     GDELSVEETF PFLEALTSLD LRPSKIDLGL LVTAYHAHGG GAPIPEFVAE SLADLVGGAH
     TSPAQPQDVV LYGFGRIGRL VARLLIEKSG SGNGLNLRAV VVRKGGKDDL VKRASLLRRD
     SVHGQFNGTI KVDDENNALI ANGNVIKFIY SNDPTTVDYT EYGIDNAILI DNTGIWRDRD
     GLSQHLRPGV AKVVLTAPGK GDVPNIVHGV NHRDIDPNER IVSCASCTTN AIVPPLKTMD
     DEFGVVRGHV ETVHSFTNDQ NLLDNFHKAD RRGRSAPFNL VLTETGAASA IAKALPDLKA
     KITGNSIRVP TPDVSVAILN LQLHREATKD EVLEHLRQES LTGALSRNLD YTAATDAVSS
     DFIGSRAACI VDANAAIVDG DTAILYVWYD NEFGYSCQVV RTVQYLSGVE YPIYPTVDAA
     AVAGAIA
//

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