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UniProtKB/Swiss-Prot entry O58320

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GYAR_PYRHO
Primary accession number O58320
Secondary accession numbers None
Integrated into Swiss-Prot on May 10, 2004
Sequence was last modified on May 10, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 52)
Name and origin of the protein
Protein name Glyoxylate reductase
Synonym EC 1.1.1.26
Gene name
Name: gyaR
OrderedLocusNames: PH0597
From
Pyrococcus horikoshii [TaxID: 53953] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; Pyrococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OT3;
DOI=10.1093/dnares/5.2.55; PubMed=9679194 [NCBI, ExPASy, EBI, Israel, Japan]
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
DNA Res. 5:55-76(1998).
[2]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH NADP.
STRAIN=OT3;
RIKEN structural genomics initiative (RSGI);
"Crystal structure of glyoxylate reductase (ph0597) from Pyrococcus horikoshii OT3, complexed with nadp (i41).";
Submitted (JUN-2006) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BA000001; BAA29686.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A71175; A71175.
RefSeq NP_142561.2; -.
3D structure databases
PDB
2DBQ; X-ray; 1.70 A; A=1-334.[ExPASy / RCSB / EBI]
2DBR; X-ray; 2.61 A; A/B/C/D/E/F=1-334.[ExPASy / RCSB / EBI]
2DBZ; X-ray; 2.45 A; A/B=1-334.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2DBQ; -.
2DBR; -.
2DBZ; -.
ModBase O58320.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0047964; Molecular function: glyoxylate reductase activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00776; -; 1.
PBIL [Tree]
InterPro IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.
PROSITE PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
PS00671; D_2_HYDROXYACID_DH_3; 1.
ProtoNet O58320.
Genome annotation databases
GeneID 1442932; -.
GenomeReviews BA000001_GR; PH0597.
KEGG pho:PH0597; -.
NMPDR fig|70601.1.peg.585; -.
Phylogenomic databases
HOGENOM O58320; -.
Genome annotation databases
CMR O58320; PH0597.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   334  334     Glyoxylate reductase. PRO_0000075949
NP_BIND   158   161  4     NADP. 
NP_BIND   180   182  3     NADP. 
NP_BIND   239   241  3     NADP. 
NP_BIND   288   290  3     NADP. 
ACT_SITE   241   241        By similarity. 
ACT_SITE   270   270        By similarity. 
ACT_SITE   288   288        Proton donor (By similarity). 
STRAND   4     9  6      
HELIX   13    20  8      
STRAND   23    27  5      
HELIX   36    42  7      
STRAND   47    51  5      
HELIX   59    63  5      
STRAND   70    76  7      
HELIX   83    88  6      
STRAND   92    94  3      
HELIX   101   117  17      
HELIX   119   127  9      
HELIX   130   133  4      
TURN   140   143  4      
STRAND   152   156  5      
HELIX   160   171  12      
STRAND   175   179  5      
HELIX   185   191  7      
HELIX   198   204  7      
STRAND   206   210  5      
TURN   216   220  5      
HELIX   224   229  6      
STRAND   235   238  4      
HELIX   242   244  3      
HELIX   247   255  9      
STRAND   258   265  8      
STRAND   268   271  4      
HELIX   275   279  5      
STRAND   283   285  3      
HELIX   294   312  19      
HELIX   325   328  4      
Sequence information
Length: 334 AA [This is the length of the unprocessed precursor] Molecular weight: 38000 Da [This is the MW of the unprocessed precursor] CRC64: C0056A354ECBE202 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKPKVFITRE IPEVGIKMLE DEFEVEVWGD EKEIPREILL KKVKEVDALV TMLSERIDKE 

        70         80         90        100        110        120 
VFENAPKLRI VANYAVGYDN IDIEEATKRG IYVTNTPDVL TDATADLAFA LLLATARHVV 

       130        140        150        160        170        180 
KGDRFVRSGE WKKRGVAWHP KWFLGYDVYG KTIGIIGLGR IGQAIAKRAK GFNMRILYYS 

       190        200        210        220        230        240 
RTRKEEVERE LNAEFKPLED LLRESDFVVL AVPLTRETYH LINEERLKLM KKTAILINIA 

       250        260        270        280        290        300 
RGKVVDTNAL VKALKEGWIA GAGLDVFEEE PYYNEELFKL DNVVLTPHIG SASFGAREGM 

       310        320        330 
AELVAKNLIA FKRGEIPPTL VNREVIKIRK PGFE
O58320 in FASTA format

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