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Protein

Homocitrate dehydratase, mitochondrial

Gene

SPBP4H10.15

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.By similarity

Catalytic activityi

(R)-2-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4-tricarboxylate + H2O.

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

Pathway:iL-lysine biosynthesis via AAA pathway

This protein is involved in step 2 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051SubstrateBy similarity
Metal bindingi394 – 3941Iron-sulfur (4Fe-4S)By similarity
Metal bindingi457 – 4571Iron-sulfur (4Fe-4S)By similarity
Metal bindingi460 – 4601Iron-sulfur (4Fe-4S)By similarity
Binding sitei484 – 4841SubstrateBy similarity
Binding sitei489 – 4891SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • glutamate metabolic process Source: PomBase
  • lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway
  • mitochondrial translation Source: PomBase
  • tricarboxylic acid cycle Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00033; UER00029.

Names & Taxonomyi

Protein namesi
Recommended name:
Homocitrate dehydratase, mitochondrial (EC:4.2.1.-)
Alternative name(s):
Aconitase 2
Gene namesi
ORF Names:SPBP4H10.15
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.15.
PomBaseiSPBP4H10.15.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • mitochondrial large ribosomal subunit Source: PomBase
  • mitochondrion Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionSequence AnalysisAdd
BLAST
Chaini31 – 918888Homocitrate dehydratase, mitochondrialPRO_0000316198Add
BLAST

Proteomic databases

MaxQBiQ9P7D4.
PaxDbiQ9P7D4.

Interactioni

Protein-protein interaction databases

BioGridi277859. 2 interactions.
MINTiMINT-4705221.

Structurei

3D structure databases

ProteinModelPortaliQ9P7D4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 2003Substrate bindingBy similarity
Regioni680 – 6812Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the aconitase/IPM isomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1048.
HOGENOMiHOG000224293.
InParanoidiQ9P7D4.
KOiK17450.
OMAiAVVANMA.
OrthoDBiEOG7X6M7Q.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR028909. L21p-like.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
PF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF141091. SSF141091. 1 hit.
SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01340. aconitase_mito. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9P7D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATFARMKLC LSGSSQAIPS KGISLVAARF QSTASRASYV TPPYEKLMGK
60 70 80 90 100
LQQVRKFLPG QKLTLAEKVL YSHLVNPEES FSGVSPSDIR GSLYLKLNPD
110 120 130 140 150
RVAMQDASAQ MALLQFMTCG LEKTMIPASI HCDHLIVGHR GANSDIPDSI
160 170 180 190 200
ANNKEIFDFL QSAAKKYGIQ FWGPGSGIIH QIVLENYAAP GGMMLGTDSH
210 220 230 240 250
TPNAGGLGMI AIGVGGADAV DAMTNTPWEL KAPKIIGVNL TGAMSGWTTP
260 270 280 290 300
KDLILHLAGK LTVRGGTGHI IEYFGPGVAS LSCTGMATVC NMGAEVGATT
310 320 330 340 350
SIFPYTDSMR RYLIATHRAE VADAASEVHS EYNYLAADTG AKYDQIIDIN
360 370 380 390 400
LSELTPSLNG PFTPDLSTPV SKFGEAIEKN KWPKKLSAGL IGSCTNSSYQ
410 420 430 440 450
DMTCVVDVVE QAISAGLKPK VPFLVTPGSE QIRATIERDG ITERLEEAGA
460 470 480 490 500
TVLANACGPC IGMWKRTDDI ASGEPNAILT SFNRNFRSRN DGNPSTMNFL
510 520 530 540 550
TSPVIVAAKI FSSDLAFDPT HDTLQTPDGK AFKFRPPQGV ELPSAGFIAG
560 570 580 590 600
DSSYIPEPNP QPVPETEVTI DPKSDRLEAL EPFEPYQGGE MENLKVAVKV
610 620 630 640 650
KGKCTTDHIS AAGKWLKYKG HLSNICNNTL IGAMNAATGE VNRAYDNGKG
660 670 680 690 700
MTIPELMWKW KKDGQPWLVV AEHNYGEGSA REHAALQPRA MNGRIILTKS
710 720 730 740 750
FARIHETNLK KQGVLPLTFV NEADYEKIDA EDKVSTRGIE QLLEGVLDQP
760 770 780 790 800
ITLVVTKKDG SVVEIPCKHT MSKDQIEFFK AGSALNLIRE KAHSGVVNQK
810 820 830 840 850
VIDSIKQQPD HYADAYIFNR HFVIAKGDQL GLPFHLKGVQ VGDTIRLDKI
860 870 880 890 900
ASFGSRDFTL FGNPYVDPSL FTIEAVVLSF PKSALSVRVK HKRRHRHDRV
910
MKHKQTYTIL RVTELKLN
Length:918
Mass (Da):99,901
Last modified:July 11, 2012 - v3
Checksum:iA17A3132B7B21D90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB83173.3.
RefSeqiNP_596189.3. NM_001022108.3.

Genome annotation databases

EnsemblFungiiSPBP4H10.15.1; SPBP4H10.15.1:pep; SPBP4H10.15.
GeneIDi2541348.
KEGGispo:SPBP4H10.15.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB83173.3.
RefSeqiNP_596189.3. NM_001022108.3.

3D structure databases

ProteinModelPortaliQ9P7D4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277859. 2 interactions.
MINTiMINT-4705221.

Proteomic databases

MaxQBiQ9P7D4.
PaxDbiQ9P7D4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP4H10.15.1; SPBP4H10.15.1:pep; SPBP4H10.15.
GeneIDi2541348.
KEGGispo:SPBP4H10.15.

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.15.
PomBaseiSPBP4H10.15.

Phylogenomic databases

eggNOGiCOG1048.
HOGENOMiHOG000224293.
InParanoidiQ9P7D4.
KOiK17450.
OMAiAVVANMA.
OrthoDBiEOG7X6M7Q.

Enzyme and pathway databases

UniPathwayiUPA00033; UER00029.

Miscellaneous databases

NextBioi20802457.
PROiQ9P7D4.

Family and domain databases

Gene3Di3.20.19.10. 1 hit.
3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
InterProiIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR006248. Aconitase_mito-like.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR028909. L21p-like.
[Graphical view]
PANTHERiPTHR11670. PTHR11670. 1 hit.
PfamiPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
PF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
PRINTSiPR00415. ACONITASE.
SUPFAMiSSF141091. SSF141091. 1 hit.
SSF52016. SSF52016. 1 hit.
SSF53732. SSF53732. 1 hit.
TIGRFAMsiTIGR01340. aconitase_mito. 1 hit.
PROSITEiPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACON2_SCHPO
AccessioniPrimary (citable) accession number: Q9P7D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 11, 2012
Last modified: July 22, 2015
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.