ID 6PGD_RAT Reviewed; 483 AA.
AC P85968;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-APR-2013, entry version 42.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=Pgd;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into
RT mammalian evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-
CC phosphogluconate to ribulose 5-phosphate and CO(2), with
CC concomitant reduction of NADP to NADPH (By similarity).
CC -!- CATALYTIC ACTIVITY: 6-phospho-D-gluconate + NADP(+) = D-ribulose
CC 5-phosphate + CO(2) + NADPH.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC step 3/3.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC family.
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DR EMBL; AABR03040409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR IPI; IPI00903436; -.
DR RefSeq; XP_002729611.1; XM_002729565.2.
DR RefSeq; XP_003754166.1; XM_003754118.1.
DR ProteinModelPortal; P85968; -.
DR PhosphoSite; P85968; -.
DR World-2DPAGE; 0004:P85968; -.
DR PaxDb; P85968; -.
DR PRIDE; P85968; -.
DR Ensembl; ENSRNOT00000018609; ENSRNOP00000018609; ENSRNOG00000030317.
DR GeneID; 100360180; -.
DR KEGG; rno:100360180; -.
DR RGD; 1583832; Pgd.
DR eggNOG; COG5059; -.
DR GeneTree; ENSGT00700000104150; -.
DR HOGENOM; HOG000255147; -.
DR HOVERGEN; HBG000029; -.
DR KO; K00033; -.
DR SABIO-RK; P85968; -.
DR UniPathway; UPA00115; UER00410.
DR ArrayExpress; P85968; -.
DR Genevestigator; P85968; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IDA:RGD.
DR GO; GO:0031406; F:carboxylic acid binding; IDA:RGD.
DR GO; GO:0050661; F:NADP binding; IDA:RGD.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR GO; GO:0019521; P:D-gluconate metabolic process; IDA:RGD.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:RGD.
DR Gene3D; 1.10.1040.10; -; 1.
DR Gene3D; 1.20.5.320; -; 1.
DR Gene3D; 3.40.50.720; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_decarbox.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR013328; DH_multihelical.
DR InterPro; IPR012284; Fibritin/6PGD_C-extension.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR SUPFAM; SSF48179; 6DGDH_C_like; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; Gluconate utilization;
KW NADP; Oxidoreductase; Pentose shunt; Reference proteome.
FT CHAIN 1 483 6-phosphogluconate dehydrogenase,
FT decarboxylating.
FT /FTId=PRO_0000349115.
FT NP_BIND 10 15 NADP (By similarity).
FT NP_BIND 33 35 NADP (By similarity).
FT NP_BIND 75 77 NADP (By similarity).
FT NP_BIND 478 481 NADP; shared with dimeric partner (By
FT similarity).
FT REGION 129 131 Substrate binding (By similarity).
FT REGION 187 188 Substrate binding (By similarity).
FT ACT_SITE 184 184 Proton acceptor (By similarity).
FT ACT_SITE 191 191 Proton donor (By similarity).
FT BINDING 103 103 NADP (By similarity).
FT BINDING 103 103 Substrate (By similarity).
FT BINDING 192 192 Substrate (By similarity).
FT BINDING 261 261 Substrate; via amide nitrogen (By
FT similarity).
FT BINDING 288 288 Substrate (By similarity).
FT BINDING 447 447 Substrate; shared with dimeric partner
FT (By similarity).
FT BINDING 453 453 Substrate; shared with dimeric partner
FT (By similarity).
FT MOD_RES 59 59 N6-acetyllysine (By similarity).
SQ SEQUENCE 483 AA; 53236 MW; 7B3F308C3E9B17D4 CRC64;
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLAKEAKGT KVIGAKSLKD
MVSKLKKPRR VILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCQDLKAKG
ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQAI AAKVGTGEPC CDWVGDEGAG
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MRHEEMAQAF EDWNKTELDS FLIEITANIL
KFQDTDGKEL LPKIRDSAGQ KGTGKWTAIS ALEYGMPVTL IGEAVFARCL SSLKEERVQA
SRKLKGPKMV QLEGSKQAFL EDVRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL
MWRGGCIIRS VFLGKIKDAF ERNPELQNLL LDDFFKSAVD DCQDSWRRVI STGVQAGIPM
PCFTTALSFY DGYRHEMLPA NLIQAQRDYF GAHTYELLSK PGEFIHTNWT GHGGSVSSSS
YNA
//
