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Protein

Homoisocitrate dehydrogenase

Gene

lys12

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

Pathwayi: L-lysine biosynthesis via AAA pathway

This protein is involved in step 4 of the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Homocitrate synthase, mitochondrial (lys4)
  2. Homocitrate dehydratase, mitochondrial (SPBP4H10.15)
  3. Homoaconitase, mitochondrial (lys2)
  4. Homoisocitrate dehydrogenase (lys12)
  5. no protein annotated in this organism
This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate, the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei97SubstrateBy similarity1
Binding sitei107SubstrateBy similarity1
Binding sitei126SubstrateBy similarity1
Sitei133Critical for catalysisBy similarity1
Sitei196Critical for catalysisBy similarity1
Metal bindingi232Magnesium or manganeseBy similarity1
Binding sitei232SubstrateBy similarity1
Metal bindingi256Magnesium or manganeseBy similarity1
Metal bindingi260Magnesium or manganeseBy similarity1

GO - Molecular functioni

GO - Biological processi

  • lysine biosynthetic process Source: PomBase
  • lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Lysine biosynthesis
LigandMagnesium, Manganese, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00033; UER00030

Names & Taxonomyi

Protein namesi
Recommended name:
Homoisocitrate dehydrogenase (EC:1.1.1.87)
Short name:
HICDH
Gene namesi
Name:lys12
ORF Names:SPAC31G5.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC31G5.04
PomBaseiSPAC31G5.04 lys12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003103741 – 362Homoisocitrate dehydrogenaseAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei81Phosphoserine1 Publication1
Modified residuei91Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO14104
PaxDbiO14104
PRIDEiO14104

PTM databases

iPTMnetiO14104

Interactioni

Protein-protein interaction databases

BioGridi279063, 19 interactors
STRINGi4896.SPAC31G5.04.1

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 15Combined sources10
Helixi18 – 30Combined sources13
Helixi34 – 36Combined sources3
Beta strandi39 – 44Combined sources6
Helixi49 – 55Combined sources7
Helixi61 – 70Combined sources10
Beta strandi72 – 78Combined sources7
Helixi92 – 99Combined sources8
Beta strandi104 – 110Combined sources7
Beta strandi116 – 118Combined sources3
Beta strandi121 – 127Combined sources7
Helixi132 – 134Combined sources3
Beta strandi137 – 141Combined sources5
Beta strandi148 – 156Combined sources9
Helixi157 – 179Combined sources23
Beta strandi190 – 195Combined sources6
Turni197 – 199Combined sources3
Helixi203 – 214Combined sources12
Helixi215 – 217Combined sources3
Helixi219 – 221Combined sources3
Beta strandi224 – 230Combined sources7
Helixi231 – 240Combined sources10
Helixi242 – 244Combined sources3
Beta strandi246 – 250Combined sources5
Helixi252 – 263Combined sources12
Helixi264 – 266Combined sources3
Helixi269 – 271Combined sources3
Beta strandi275 – 277Combined sources3
Beta strandi282 – 284Combined sources3
Turni292 – 296Combined sources5
Helixi303 – 315Combined sources13
Helixi319 – 335Combined sources17
Helixi341 – 343Combined sources3
Helixi349 – 359Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TY3X-ray1.85A/B1-362[»]
3TY4X-ray1.55A/B1-362[»]
ProteinModelPortaliO14104
SMRiO14104
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000021111
InParanoidiO14104
KOiK05824
OMAiECLYVKQ
OrthoDBiEOG092C2YAZ
PhylomeDBiO14104

Family and domain databases

InterProiView protein in InterPro
IPR019818 IsoCit/isopropylmalate_DH_CS
IPR024084 IsoPropMal-DH-like_dom
PfamiView protein in Pfam
PF00180 Iso_dh, 1 hit
SMARTiView protein in SMART
SM01329 Iso_dh, 1 hit
PROSITEiView protein in PROSITE
PS00470 IDH_IMDH, 1 hit

Sequencei

Sequence statusi: Complete.

O14104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSATRRIVLG LIPADGIGKE VVPAARRLME NLPAKHKLKF DFIDLDAGWG
60 70 80 90 100
TFERTGKALP ERTVERLKTE CNAALFGAVQ SPTHKVAGYS SPIVALRKKM
110 120 130 140 150
GLYANVRPVK SLDGAKGKPV DLVIVRENTE CLYVKEERMV QNTPGKRVAE
160 170 180 190 200
AIRRISEEAS TKIGKMAFEI AKSRQKIRES GTYSIHKKPL VTIIHKSNVM
210 220 230 240 250
SVTDGLFRES CRHAQSLDPS YASINVDEQI VDSMVYRLFR EPECFDVVVA
260 270 280 290 300
PNLYGDILSD GAASLIGSLG LVPSANVGDN FVMSEPVHGS APDIAGRGIA
310 320 330 340 350
NPVATFRSVA LMLEFMGHQD AAADIYTAVD KVLTEGKVLT PDLGGKSGTN
360
EITDAVLANI HN
Length:362
Mass (Da):39,256
Last modified:January 1, 1998 - v1
Checksum:i85865AFD69BCE773
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA Translation: CAB11688.1
PIRiT38621
RefSeqiNP_594004.1, NM_001019430.2

Genome annotation databases

EnsemblFungiiSPAC31G5.04.1; SPAC31G5.04.1:pep; SPAC31G5.04
GeneIDi2542609
KEGGispo:SPAC31G5.04

Similar proteinsi

Entry informationi

Entry nameiLYS12_SCHPO
AccessioniPrimary (citable) accession number: O14104
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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