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P39119

- CISY_BACSU

UniProt

P39119 - CISY_BACSU

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Protein

Citrate synthase 1

Gene

citA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 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.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei252 – 2521PROSITE-ProRule annotation
Active sitei307 – 3071PROSITE-ProRule annotation

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:BSU09440-MONOMER.
RETL1328306-WGS:GSTH-2193-MONOMER.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase 1 (EC:2.3.3.16)
Alternative name(s):
Citrate synthase I
Gene namesi
Name:citA
Ordered Locus Names:BSU09440
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU09440. [Micado]

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071E → D: 5-fold increase in activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Citrate synthase 1PRO_0000169928Add
BLAST

Proteomic databases

PaxDbiP39119.
PRIDEiP39119.

Expressioni

Inductioni

By decoyinine and nutrient depletion.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi224308.BSU09440.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi12 – 209Combined sources
Turni21 – 244Combined sources
Beta strandi25 – 284Combined sources
Helixi33 – 397Combined sources
Helixi42 – 5110Combined sources
Helixi57 – 7014Combined sources
Helixi75 – 839Combined sources
Beta strandi86 – 883Combined sources
Helixi90 – 10112Combined sources
Helixi112 – 13322Combined sources
Helixi148 – 1569Combined sources
Helixi162 – 17615Combined sources
Helixi182 – 19110Combined sources
Turni192 – 1943Combined sources
Helixi197 – 20913Combined sources
Helixi218 – 2258Combined sources
Helixi233 – 24210Combined sources
Helixi260 – 27112Combined sources
Turni272 – 2743Combined sources
Helixi277 – 29620Combined sources
Helixi307 – 31610Combined sources
Helixi321 – 3233Combined sources
Helixi324 – 34320Combined sources
Turni344 – 3463Combined sources
Beta strandi353 – 3564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C6XX-ray3.40A/B/C/D2-364[»]
ProteinModelPortaliP39119.
SMRiP39119. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39119.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP39119.
KOiK01647.
OrthoDBiEOG6P8TP4.
PhylomeDBiP39119.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. 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.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39119-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVHYGLKGIT CVETSISHID GEKGRLIYRG HHAKDIALNH SFEEAAYLIL
60 70 80 90 100
FGKLPSTEEL QVFKDKLAAE RNLPEHIERL IQSLPNNMDD MSVLRTVVSA
110 120 130 140 150
LGENTYTFHP KTEEAIRLIA ITPSIIAYRK RWTRGEQAIA PSSQYGHVEN
160 170 180 190 200
YYYMLTGEQP SEAKKKALET YMILATEHGM NASTFSARVT LSTESDLVSA
210 220 230 240 250
VTAALGTMKG PLHGGAPSAV TKMLEDIGEK EHAEAYLKEK LEKGERLMGF
260 270 280 290 300
GHRVYKTKDP RAEALRQKAE EVAGNDRDLD LALHVEAEAI RLLEIYKPGR
310 320 330 340 350
KLYTNVEFYA AAVMRAIDFD DELFTPTFSA SRMVGWCAHV LEQAENNMIF
360
RPSAQYTGAI PEEVLS
Length:366
Mass (Da):40,952
Last modified:June 16, 2009 - v2
Checksum:iADF8AB7CFE837861
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → V in AAA20936. (PubMed:8045898)Curated
Sequence conflicti94 – 941L → V in CAA74489. (PubMed:9579061)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05256 Genomic DNA. Translation: AAA20936.1.
Y14082 Genomic DNA. Translation: CAA74489.1.
AL009126 Genomic DNA. Translation: CAB12783.2.
PIRiI40380.
RefSeqiNP_388825.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12783; CAB12783; BSU09440.
GeneIDi936270.
KEGGibsu:BSU09440.
PATRICi18973584. VBIBacSub10457_0986.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05256 Genomic DNA. Translation: AAA20936.1 .
Y14082 Genomic DNA. Translation: CAA74489.1 .
AL009126 Genomic DNA. Translation: CAB12783.2 .
PIRi I40380.
RefSeqi NP_388825.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C6X X-ray 3.40 A/B/C/D 2-364 [» ]
ProteinModelPortali P39119.
SMRi P39119. Positions 2-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU09440.

Proteomic databases

PaxDbi P39119.
PRIDEi P39119.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12783 ; CAB12783 ; BSU09440 .
GeneIDi 936270.
KEGGi bsu:BSU09440.
PATRICi 18973584. VBIBacSub10457_0986.

Organism-specific databases

GenoListi BSU09440. [Micado ]

Phylogenomic databases

eggNOGi COG0372.
HOGENOMi HOG000021225.
InParanoidi P39119.
KOi K01647.
OrthoDBi EOG6P8TP4.
PhylomeDBi P39119.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .
BioCyci BSUB:BSU09440-MONOMER.
RETL1328306-WGS:GSTH-2193-MONOMER.

Miscellaneous databases

EvolutionaryTracei P39119.

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProi 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.
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].
    Strain: 168 / SMY.
  2. "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus subtilis chromosome contains several dysfunctional genes, the glyB marker, many genes encoding transporter proteins, and the ubiquitous hit gene."
    Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H., Venema G., Bron S.
    Microbiology 144:859-875(1998) [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. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 94.

Entry informationi

Entry nameiCISY_BACSU
AccessioniPrimary (citable) accession number: P39119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: November 26, 2014
This is version 108 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

3D-structure, Allosteric enzyme, Complete proteome, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3