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Q58991 (AKSF_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homoisocitrate dehydrogenase
Short name=HICDH
EC=1.1.1.87
Alternative name(s):
Isohomocitrate dehydrogenase
Short name=IHDH
NAD-dependent threo-isohomocitrate dehydrogenase
Gene names
Name:aksF
Synonyms:icd
Ordered Locus Names:MJ1596
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NAD-dependent oxidation and decarboxylation of (2R,3S)-homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate), (2R,3S)-homo(2)-isocitrate and (2R,3S)-homo(3)-isocitrate, into 2-oxoadipate, 2-oxopimelate, and 2-oxosuberate, respectively. This last compound is a precursor to coenzyme B and biotin in methanoarchaea. Is also able to produce 2-oxoazelate from (2R,3S)-homo(4)-isocitrate. Is not able to use NADP as an oxidant. Ref.1

Catalytic activity

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH. Ref.1

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Organic acid metabolism; 2-oxosuberate biosynthesis.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Biophysicochemical properties

Kinetic parameters:

KM=0.037 mM for (2R,3S)-homoisocitrate Ref.3

KM=0.016 mM for (2R,3S)-homo(2)-isocitrate

KM=0.021 mM for (2R,3S)-homo(3)-isocitrate

Vmax=2.6 µmol/min/mg enzyme with (2R,3S)-homoisocitrate as substrate

Vmax=8.7 µmol/min/mg enzyme with (2R,3S)-homo(2)-isocitrate as substrate

Vmax=7.1 µmol/min/mg enzyme with (2R,3S)-homo(3)-isocitrate as substrate

Temperature dependence:

Stable at 100 degrees Celsius for 10 min.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Homoisocitrate dehydrogenase
PRO_0000083574

Sites

Metal binding2131Magnesium or manganese By similarity
Metal binding2371Magnesium or manganese By similarity
Metal binding2411Magnesium or manganese By similarity
Binding site811Substrate By similarity
Binding site871Substrate By similarity
Binding site971Substrate By similarity
Binding site1281Substrate By similarity
Binding site2131Substrate By similarity
Site1351Critical for catalysis By similarity
Site1811Critical for catalysis By similarity

Amino acid modifications

Modified residue811Phosphoserine By similarity

Experimental info

Sequence conflict771K → Q in AAB99614. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q58991 [UniParc].

Last modified March 24, 2009. Version 3.
Checksum: 20D7BF9FDA451116

FASTA34738,536
        10         20         30         40         50         60 
MMKVCVIEGD GIGKEVIPEA IKILNELGEF EIIKGEAGLE CLKKYGNALP EDTIEKAKEA 

        70         80         90        100        110        120 
DIILFGAITS PKPGEVKNYK SPIITLRKMF HLYANVRPIN NFGIGQLIGK IADYEFLNAK 

       130        140        150        160        170        180 
NIDIVIIREN TEDLYVGRER LENDTAIAER VITRKGSERI IRFAFEYAIK NNRKKVSCIH 

       190        200        210        220        230        240 
KANVLRITDG LFLEVFNEIK KHYNIEADDY LVDSTAMNLI KHPEKFDVIV TTNMFGDILS 

       250        260        270        280        290        300 
DEASALIGGL GLAPSANIGD DKALFEPVHG SAPDIAGKGI ANPMASILSI AMLFDYIGEK 

       310        320        330        340 
EKGDLIREAV KYCLINKKVT PDLGGDLKTK DVGDEILNYI RKKLKGY

« Hide

References

« Hide 'large scale' references
[1]"Methanogen homoaconitase catalyzes both hydrolyase reactions in coenzyme B biosynthesis."
Drevland R.M., Jia Y., Palmer D.R.J., Graham D.E.
J. Biol. Chem. 283:28888-28896(2008) [PubMed: 18765671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[3]"Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea."
Howell D.M., Graupner M., Xu H., White R.H.
J. Bacteriol. 182:5013-5016(2000) [PubMed: 10940051] [Abstract]
Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		EU447775 Genomic DNA. Translation: ACA28837.1.
L77117 Genomic DNA. Translation: AAB99614.1.
RefSeqNP_248605.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58991.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1452504.
GenomeReviewsGene locus MJ1596 in contig L77117_GR.
KEGGmja:MJ_1596.
NMPDRfig|243232.1.peg.1642.
TIGRMJ1596.

Phylogenomic databases

HOGENOMHBG518924.
OMAKPTELKN.
ProtClustDBCLSK876638.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2004.
MJAN243232:MJ_1596-MONOMER.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR011828. LEU3_arc.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KOK10978.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR02088. LEU3_arch. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAKSF_METJA
AccessionPrimary (citable) accession number: Q58991
Secondary accession number(s): B1PL93
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 24, 2009
Last modified: November 16, 2011
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents