439aa long hypothetical malate oxidoreductase (NAD) [malic enzyme] - Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Preferred order of sections

Names and origin

Protein names

Submitted name:
439aa long hypothetical malate oxidoreductase (NAD) [malic enzyme] EMBL BAA30378.1

Gene names

Ordered Locus Names:

PH1275

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	NAD PDB 2DVM Nucleotide-binding PDB 2DVM
Technical term	3D-structure PDB 2DVM PDB 1WW8 Complete proteome
Gene Ontology (GO)
Biological process	malate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (oxaloacetate-decarboxylating) activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

196 – 197

2

NAD PDB 2DVM

Nucleotide binding

326 – 328

3

NAD PDB 2DVM

Sites

Binding site

74

1

NAD PDB 2DVM

Binding site

219

1

NAD PDB 2DVM

Binding site

297

1

NAD PDB 2DVM

Sequences

Sequence

Length

Mass (Da)

Tools

O59029 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 64CD15417DE9C669
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FASTA

439

48,004

        10         20         30         40         50         60 
MIREKALEFH KNNFPGNGKI EVIPKVSLES REELTLAYTP GVAEPCKEIA RDPGKVYEYT 

        70         80         90        100        110        120 
SKGNLVAVVS DGSRILGLGN IGPLAGLPVM EGKALLFKRF GGVDAFPIMI KEQEPNKFID 

       130        140        150        160        170        180 
IVKAIAPTFG GINLEDIASP KCFYILERLR EELDIPVFHD DQQGTAAVVL AGLLNALKVV 

       190        200        210        220        230        240 
GKKISEITLA LFGAGAAGFA TLRILTEAGV KPENVRVVEL VNGKPRILTS DLDLEKLFPY 

       250        260        270        280        290        300 
RGWLLKKTNG ENIEGGPQEA LKDADVLISF TRPGPGVIKP QWIEKMNEDA IVFPLANPVP 

       310        320        330        340        350        360 
EILPEEAKKA GARIVATGRS DYPNQINNLL GFPGIFRGAL DVRARTITDS MIIAAAKAIA 

       370        380        390        400        410        420 
SIVEEPSEEN IIPSPLNPIV YAREARAVAE EAMKEGVART KVKGEWVEEH TIRLIEFYEN 

       430 
VIAPINKKRR EYSKAITRA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." 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. Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 and OT3.
[2]	"Crystal Structure of malic enzyme from Pyrococcus horikoshii Ot3." Lokanath N.K., Kunishima N. Submitted (JAN-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
[3]	"NAD complex structure of PH1275 protein from Pyrococcus horikoshii." Lokanath N.K., Mizutani H., Kunishima N. Submitted (JUL-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30378.1.

PIR

H71072.

RefSeq

NP_143165.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WW8	X-ray	2.50	A/B	1-439	[»]
2DVM	X-ray	1.60	A/B/C/D	1-439	[»]

ProteinModelPortal

O59029.

SMR

O59029. Positions 2-439.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000000115; EBPYRP00000000115; EBPYRG00000000115.

GeneID

1443599.

GenomeReviews

Gene locus PH1275 in contig BA000001_GR.

KEGG

pho:PH1275.

NMPDR

fig|70601.1.peg.1252.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022899.

HOGENOM

HBG285702.

OMA

LDIPVWH.

PhylomeDB

O59029.

ProtClustDB

CLSK306482.

Enzyme and pathway databases

BioCyc

PHOR70601:PH1275-MONOMER.

Family and domain databases

InterPro

IPR015884. Malic_enzyme_CS.
IPR012301. Malic_N.
IPR012302. Malic_NAD-bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.10380. G3DSA:3.40.50.10380. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF00390. malic. 2 hits.
PF03949. Malic_M. 1 hit.
[Graphical view]

PIRSF

PIRSF000106. ME. 1 hit.

SMART

SM00919. Malic_M. 1 hit.
[Graphical view]

PROSITE

PS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O59029_PYRHO

Accession

Primary (citable) accession number: O59029

Entry history

Integrated into UniProtKB/TrEMBL:	August 1, 1998
Last sequence update:	August 1, 1998
Last modified:	December 14, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)