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P09339 (ACON_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aconitate hydratase
Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
Name:citB
Ordered Locus Names:BSU18000
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length909 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.

Catalytic activity

Citrate = isocitrate.

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.

Subunit structure

Monomer.

Induction

By citrate, decoyinine and nutrient depletion.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 909908Aconitate hydratase
PRO_0000076655

Sites

Metal binding4501Iron-sulfur (4Fe-4S) By similarity
Metal binding5161Iron-sulfur (4Fe-4S) By similarity
Metal binding5191Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict43 – 453SKL → FEA in AAA22316. Ref.4
Sequence conflict1191G → V no nucleotide entry Ref.3

Sequences

Sequence LengthMass (Da)Tools
P09339 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 9545E734F2BCF735

FASTA90999,334
        10         20         30         40         50         60 
MANEQKTAAK DVFQARKTFT TNGKTYHYYS LKALEDSGIG KVSKLPYSIK VLLESVLRQV 

        70         80         90        100        110        120 
DGFVIKKEHV ENLAKWGTAE LKDIDVPFKP SRVILQDFTG VPAVVDLASL RKAMAAVGGD 

       130        140        150        160        170        180 
PDKINPEIPV DLVIDHSVQV DKAGTEDALA VNMDLEFERN AERYKFLSWA KKAFNNYQAV 

       190        200        210        220        230        240 
PPATGIVHQV NLEFLASVVH AIEEDGELVT YPDTLVGTDS HTTMINGIGV LGWGVGGIEA 

       250        260        270        280        290        300 
EAGMLGQPSY FPVPEVIGAK LVGKLPNGTT ATDLALKVTQ VLREKGVVGK FVEFFGPGIA 

       310        320        330        340        350        360 
ELPLADRATI ANMAPEYGAT CGFFPVDEEA LNYLRLTGRD PEHIDVVEAY CRSNGLFYTP 

       370        380        390        400        410        420 
DAEDPQFTDV VEIDLSQIEA NLSGPKRPQD LIPLSAMQET FKKQLVSPAG NQGFGLNAEE 

       430        440        450        460        470        480 
ENKEIKFKLL NGEETVMKTG AIAIAAITSC TNTSNPYVLI GAGLVAKKAV ELGLKVPNYV 

       490        500        510        520        530        540 
KTSLAPGSKV VTGYLVNSGL LPYMKELGFN LVGYGCTTCI GNSGPLSPEI EEAVAKNDLL 

       550        560        570        580        590        600 
ITSVLSGNRN FEGRIHPLVK GNYLASPPLV VAYALAGTVN INLKTDPIGV GKDGQNVYFN 

       610        620        630        640        650        660 
DIWPSMDEIN ALVKQTVTPE LFRKEYETVF DDNKRWNEIE TTDEALYKWD NDSTYIQNPP 

       670        680        690        700        710        720 
FFEEMSVEPG KVEPLKGLRV VGKFGDSVTT DHISPAGAIG KDTPAGKYLQ EKGVSPRDFN 

       730        740        750        760        770        780 
SYGSRRGNHE VMMRGTFANI RIKNQIAPGT EGGFTTYWPT GEVTSIYDAC MKYKEDKTGL 

       790        800        810        820        830        840 
VVLAGKDYGM GSSRDWAAKG TNLLGIRTVI AESFERIHRS NLVFMGVLPL QFKQGENADT 

       850        860        870        880        890        900 
LGLTGKEVIE VDVDETVRPR DLVTVRAINE DGNVTTFEAV VRFDSEVEID YYRHGGILQM 


VLREKMKQS

« Hide

References

« Hide 'large scale' references
[1]"New genes in the 170 degrees region of the Bacillus subtilis genome encode DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid transporter."
Rose M., Entian K.-D.
Microbiology 142:3097-3101(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"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. expand/collapse author list , 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.
[3]Wilde R.J.
Thesis (1988), University of Sheffield, United Kingdom
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-141.
[4]"Purification of aconitase from Bacillus subtilis and correlation of its N-terminal amino acid sequence with the sequence of the citB gene."
Dingman D.W., Sonenshein A.L.
J. Bacteriol. 169:3062-3067(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45, PROTEIN SEQUENCE OF 2-8.
[5]Sonenshein A.L.
Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z73234 Genomic DNA. Translation: CAA97599.1.
AL009126 Genomic DNA. Translation: CAB13684.1.
M16776 Genomic DNA. Translation: AAA22316.1.
PIRG69599.
RefSeqNP_389683.1. NC_000964.3.

3D structure databases

ProteinModelPortalP09339.
SMRP09339. Positions 10-907.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU18000.

Proteomic databases

PaxDbP09339.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13684; CAB13684; BSU18000.
GeneID938140.
KEGGbsu:BSU18000.
PATRIC18975429. VBIBacSub10457_1906.

Organism-specific databases

GenoListBSU18000. [Micado]

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000025704.
KOK01681.
OMADEALYKW.
ProtClustDBPRK09277.

Enzyme and pathway databases

BioCycBSUB:BSU18000-MONOMER.
UniPathwayUPA00223; UER00718.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR006249. Aconitase/Fe_reg_prot_2.
IPR015934. Aconitase/Fe_reg_prot_2/AcnD.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF1. PTHR11670:SF1. 1 hit.
PfamPF00330. Aconitase. 1 hit.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01341. aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACON_BACSU
AccessionPrimary (citable) accession number: P09339
Secondary accession number(s): Q45059
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 108 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents