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Protein

Citrate synthase, mitochondrial

Gene

cit-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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 sitei352 – 3521PROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:cit-1
ORF Names:B1D1.330, NCU01692
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 6, Linkage Group II

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 469436Citrate synthase, mitochondrialPRO_0000005480Add
BLAST

Proteomic databases

PRIDEiP34085.

Expressioni

Developmental stagei

Abundant after 6-12 hours of growth. It is not significantly expressed after 24 hours, which is several hours after entering the stationary phase of growth.

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU01692.1.

Structurei

3D structure databases

ProteinModelPortaliP34085.
SMRiP34085. Positions 33-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiP34085.
KOiK01647.
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.

P34085-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPVMRLGSA ALRSSIHLTS RQTAFTAARC YSSKTQTLKE RFAELLPENI
60 70 80 90 100
EKIKALRKEH GSKVVDKVTL DQVYGGARGI KCLVWEGSVL DAEEGIRFRG
110 120 130 140 150
KTIPECQELL PKAPGGKEPL PEGLFWLLLT GEVPSEQQVR DLSAEWAARS
160 170 180 190 200
DVPKFIEELI DRCPSDLHPM AQLSLAVTAL EHTSSFARAY AKGINKKEYW
210 220 230 240 250
GYTFEDSMDL IAKLPTIAAR IYQNVFKGGK VAAVQKDKDY SFNFANQLGF
260 270 280 290 300
GDNKDFVELL RLYLTIHTDH EGGNVSAHTT HLVGSALSSP FLSVAAGLNG
310 320 330 340 350
LAGPLHGLAN QEVLNWLTEM KKVIGDDLSD EAITKYLWDT LNAGRVVPGY
360 370 380 390 400
GHAVLRKTDP RYSAQRKFAQ EHLPEDPMFQ LVSQVYKIAP KVLTEHGKTK
410 420 430 440 450
NPYPNVDAHS GVLLQHYGLT EANYYTVLFG VSRAIGVLPQ LIIDRAVGAP
460
IERPKSYSTD KWIEICKKL
Length:469
Mass (Da):51,989
Last modified:April 30, 2003 - v2
Checksum:iC14FFDDE07D345FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti351 – 3511G → A in AAA16630 (PubMed:7904043).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84187 Unassigned DNA. Translation: AAA16630.1.
AL355927 Genomic DNA. Translation: CAB91282.1.
CM002237 Genomic DNA. Translation: EAA27662.1.
PIRiS41563.
RefSeqiXP_956898.1. XM_951805.2.
UniGeneiNcr.20011.

Genome annotation databases

EnsemblFungiiEFNCRT00000001887; EFNCRP00000001887; EFNCRG00000001885.
GeneIDi3873020.
KEGGincr:NCU01692.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84187 Unassigned DNA. Translation: AAA16630.1.
AL355927 Genomic DNA. Translation: CAB91282.1.
CM002237 Genomic DNA. Translation: EAA27662.1.
PIRiS41563.
RefSeqiXP_956898.1. XM_951805.2.
UniGeneiNcr.20011.

3D structure databases

ProteinModelPortaliP34085.
SMRiP34085. Positions 33-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU01692.1.

Proteomic databases

PRIDEiP34085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000001887; EFNCRP00000001887; EFNCRG00000001885.
GeneIDi3873020.
KEGGincr:NCU01692.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiP34085.
KOiK01647.
OrthoDBiEOG7WQ82G.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

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. "Characterization of the cit-1 gene from Neurospora crassa encoding the mitochondrial form of citrate synthase."
    Ferea T., Contreras E.T., Oung T., Bowman E.J., Bowman B.J.
    Mol. Gen. Genet. 242:105-110(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 74A.
  2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiCISY_NEUCR
AccessioniPrimary (citable) accession number: P34085
Secondary accession number(s): Q7RY26, Q9P688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: April 30, 2003
Last modified: April 1, 2015
This is version 116 of the entry and version 2 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.