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Protein

Citrate synthase, mitochondrial

Gene

citA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei310 – 3101PROSITE-ProRule annotation
Active sitei356 – 3561PROSITE-ProRule annotation
Active sitei411 – 4111PROSITE-ProRule annotation

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: ASPGD

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BRENDAi2.3.3.16. 517.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:citA
ORF Names:AN8275
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence AnalysisAdd
BLAST
Chaini36 – 474439Citrate synthase, mitochondrialPRO_0000005477Add
BLAST

Proteomic databases

PRIDEiO00098.

Structurei

3D structure databases

ProteinModelPortaliO00098.
SMRiO00098. Positions 39-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiO00098.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG7WQ82G.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O00098-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTLRLSTS ALRSSTLAGK PVVQSVAFNG LRCYSTGKTK SLKETFADKL
60 70 80 90 100
PGELEKVKKL RKEHGNKVIG ELTLDQAYGG ARGVKCLVWE GSVLDSEEGI
110 120 130 140 150
RFRGLTIPEC QKLLPKAPGG EEPLPEGLFW LLLTGEVPSE QQVRDLSAEW
160 170 180 190 200
AARSDLPKFI EELIDRCPST LHPMAQFSLA VTALEHESAF AKAYAKGINK
210 220 230 240 250
KEYWHYTFED SMDLIAKLPT IAAKIYRNVF KDGKVAPIQK DKDYSYNLAN
260 270 280 290 300
QLGFADNKDF VELMRLYLTI HSDHEGGNVS AHTTHLVGSA LSSPMLSLAA
310 320 330 340 350
GLNGLAGPLH GLANQEVLNW LTEMKKVVGN DLSDQSIKDY LWSTLNAGRV
360 370 380 390 400
VPGYGHAVLR KTDPRYTSQR EFALRKLPDD PMFKLVSQVY KIAPGVLTEH
410 420 430 440 450
GKTKNPYPNV DAHSGVLLQY YGLTEANYYT VLFGVSRALG VLPQLIIDRA
460 470
FGAPIERPKS FSTEAYAKLV GAKL
Length:474
Mass (Da):52,227
Last modified:April 30, 2007 - v3
Checksum:i2CA133032DE5C3EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671C → V in AAC49728 (PubMed:9163747).Curated
Sequence conflicti167 – 1671C → V in AAM22645 (PubMed:16372000).Curated
Sequence conflicti194 – 1941Y → T in AAC49728 (PubMed:9163747).Curated
Sequence conflicti194 – 1941Y → T in AAM22645 (PubMed:16372000).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89675 Genomic DNA. Translation: AAC49728.3.
AF468824 mRNA. Translation: AAM22645.1.
AACD01000145 Genomic DNA. Translation: EAA59013.1.
BN001302 Genomic DNA. Translation: CBF74260.1.
RefSeqiXP_681544.1. XM_676452.1.

Genome annotation databases

EnsemblFungiiCADANIAT00004335; CADANIAP00004335; CADANIAG00004335.
GeneIDi2868998.
KEGGiani:AN8275.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89675 Genomic DNA. Translation: AAC49728.3.
AF468824 mRNA. Translation: AAM22645.1.
AACD01000145 Genomic DNA. Translation: EAA59013.1.
BN001302 Genomic DNA. Translation: CBF74260.1.
RefSeqiXP_681544.1. XM_676452.1.

3D structure databases

ProteinModelPortaliO00098.
SMRiO00098. Positions 39-473.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO00098.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00004335; CADANIAP00004335; CADANIAG00004335.
GeneIDi2868998.
KEGGiani:AN8275.2.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiO00098.
KOiK01647.
OMAiITDYLWS.
OrthoDBiEOG7WQ82G.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BRENDAi2.3.3.16. 517.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the citA gene encoding the mitochondrial citrate synthase of Aspergillus nidulans."
    Park B.W., Han K.H., Lee C.Y., Lee C.H., Maeng P.J.
    Mol. Cells 7:290-295(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. Seo S.W., Lee C.H., Maeng P.J.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiCISY_EMENI
AccessioniPrimary (citable) accession number: O00098
Secondary accession number(s): C8V3P7, Q5ATV5, Q8NKF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: April 30, 2007
Last modified: March 31, 2015
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.