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P39120

- CISY2_BACSU

UniProt

P39120 - CISY2_BACSU

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Protein
Citrate synthase 2
Gene
citZ, citA2, BSU29140
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect.

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei257 – 2571 By similarity
Active sitei308 – 3081 By similarity

GO - Molecular functioni

  1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

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

BioCyciBSUB:BSU29140-MONOMER.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase 2 (EC:2.3.3.16)
Alternative name(s):
Citrate synthase II
Gene namesi
Name:citZ
Synonyms:citA2
Ordered Locus Names:BSU29140
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU29140. [Micado]

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Citrate synthase 2
PRO_0000169929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei284 – 2841Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP39120.
PRIDEiP39120.

PTM databases

PhosSiteiP0802203.

Expressioni

Inductioni

By decoyinine and nutrient depletion.

Interactioni

Subunit structurei

Homodimer Inferred.

Protein-protein interaction databases

IntActiP39120. 1 interaction.
MINTiMINT-8365474.
STRINGi224308.BSU29140.

Structurei

3D structure databases

ProteinModelPortaliP39120.
SMRiP39120. Positions 3-371.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
KOiK01647.
OMAiKFPTIVA.
OrthoDBiEOG6P8TP4.
PhylomeDBiP39120.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39120-1 [UniParc]FASTAAdd to Basket

« Hide

MTATRGLEGV VATTSSVSSI IDDTLTYVGY DIDDLTENAS FEEIIYLLWH    50
LRLPNKKELE ELKQQLAKEA AVPQEIIEHF KSYSLENVHP MAALRTAISL 100
LGLLDSEADT MNPEANYRKA IRLQAKVPGL VAAFSRIRKG LEPVEPREDY 150
GIAENFLYTL NGEEPSPIEV EAFNKALILH ADHELNASTF TARVCVATLS 200
DIYSGITAAI GALKGPLHGG ANEGVMKMLT EIGEVENAEP YIRAKLEKKE 250
KIMGFGHRVY KHGDPRAKHL KEMSKRLTNL TGESKWYEMS IRIEDIVTSE 300
KKLPPNVDFY SASVYHSLGI DHDLFTPIFA VSRMSGWLAH ILEQYDNNRL 350
IRPRADYTGP DKQKFVPIEE RA 372
Length:372
Mass (Da):41,729
Last modified:July 15, 1998 - v2
Checksum:iF19D7D4561EA55A7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391A → R in AAA96341. 1 Publication
Sequence conflicti268 – 2692KH → ND in AAA96341. 1 Publication
Sequence conflicti332 – 3321S → R in AAA96341. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05257 Genomic DNA. Translation: AAA96341.1.
AF008220 Genomic DNA. Translation: AAC00345.1.
AL009126 Genomic DNA. Translation: CAB14874.1.
PIRiG69600.
RefSeqiNP_390792.1. NC_000964.3.
WP_004398810.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB14874; CAB14874; BSU29140.
GeneIDi937381.
KEGGibsu:BSU29140.
PATRICi18977722. VBIBacSub10457_3049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05257 Genomic DNA. Translation: AAA96341.1 .
AF008220 Genomic DNA. Translation: AAC00345.1 .
AL009126 Genomic DNA. Translation: CAB14874.1 .
PIRi G69600.
RefSeqi NP_390792.1. NC_000964.3.
WP_004398810.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P39120.
SMRi P39120. Positions 3-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P39120. 1 interaction.
MINTi MINT-8365474.
STRINGi 224308.BSU29140.

PTM databases

PhosSitei P0802203.

Proteomic databases

PaxDbi P39120.
PRIDEi P39120.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14874 ; CAB14874 ; BSU29140 .
GeneIDi 937381.
KEGGi bsu:BSU29140.
PATRICi 18977722. VBIBacSub10457_3049.

Organism-specific databases

GenoListi BSU29140. [Micado ]

Phylogenomic databases

eggNOGi COG0372.
HOGENOMi HOG000021225.
KOi K01647.
OMAi KFPTIVA.
OrthoDBi EOG6P8TP4.
PhylomeDBi P39120.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
BioCyci BSUB:BSU29140-MONOMER.

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProi IPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PIRSFi PIRSF001369. Citrate_synth. 1 hit.
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
TIGRFAMsi TIGR01800. cit_synth_II. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of two distinct Bacillus subtilis citrate synthase genes."
    Jin S., Sonenshein A.L.
    J. Bacteriol. 176:4669-4679(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-21 AND 228-237.
    Strain: 168 / SMY.
  2. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.

Entry informationi

Entry nameiCISY2_BACSU
AccessioniPrimary (citable) accession number: P39120
Secondary accession number(s): O34435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 15, 1998
Last modified: September 3, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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