Aconitate hydratase precursor - Deinococcus radiodurans

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Q9RTN7 (ACON_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aconitate hydratase
Short name=Aconitase
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase

Gene names

Name:	acn
Ordered Locus Names:	DR_1720

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	906 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.
Catalytic activity	Citrate = isocitrate. UniProtKB P09339
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. UniProtKB P09339
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. UniProtKB P09339
Subunit structure	Monomer By similarity. UniProtKB P09339
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from electronic annotation. Source: EC citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

Ref.2

PRO_0000370734

Chain

3 – 906

904

Aconitate hydratase Ref.2

PRO_0000370735

Sites

Metal binding

441

Iron-sulfur (4Fe-4S) By similarity UniProtKB P09339

Metal binding

507

Iron-sulfur (4Fe-4S) By similarity UniProtKB P09339

Metal binding

510

Iron-sulfur (4Fe-4S) By similarity UniProtKB P09339

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RTN7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 64058AB470F010F0
Show »

FASTA

906

98,002

        10         20         30         40         50         60 
MSDKAMNLFG ARDTLQVPGS DKKLYFYNLN KLQGHDVSRL PVSIKVLLES VLREANDYDV 

        70         80         90        100        110        120 
RREDVETVAG WSATNPEVEI PFKPARVILQ DFTGVPAVVD LAAMRSAMVK LGGDPSKINP 

       130        140        150        160        170        180 
LIPVDLVIDH SVQVDEFGTE FALANNMALE FERNRERYEF LRWGQQAFDN FGVVPPASGI 

       190        200        210        220        230        240 
VHQVNLEYLA KGVQSRAEDD GEVVYPDSLV GTDSHTTMIN GLGIVGWGVG GIEAEAVMLG 

       250        260        270        280        290        300 
QPIYMLMPEV IGFKITGAMP EGATATDLAL RVTQMLREKG VVGKFVEFYG AGLSNMTLPD 

       310        320        330        340        350        360 
RATIANMAPE YGATMGFFPV DDEALRYLRR TGRLEDEIGL VEAYYKAQGM FRTDETPDPV 

       370        380        390        400        410        420 
FTDTIELDLA TIVPSLAGPK RPQDRVNLSD MHSVFNEALT APVKNRGFEL GSDKLDAQGT 

       430        440        450        460        470        480 
IGGTDIKIGH GAVTLASITS CTNTSNPSVL IAAGLVAKKA VEKGLKTKPW VKTSLAPGSR 

       490        500        510        520        530        540 
VVTEYLETAG LQQYLDQIGF NTVGYGCMTC IGNSGPLPEP VVEAIQEGDL VVASVLSGNR 

       550        560        570        580        590        600 
NFEGRVNPHI KANYLASPPL VVAYALAGTV VNDIVNDAIG QDSNGQDVFL KDIWPTNAEI 

       610        620        630        640        650        660 
QEAMDRSINA EMFKKVYDGI EKSNADWNAI PVAEGALFDW KEDSTYIQNP PFFDTLAGGA 

       670        680        690        700        710        720 
HEIESIKGAR ALVKVGDSVT TDHISPAGSF KADTPAGRYL TERGIAPKDF NSYGSRRGND 

       730        740        750        760        770        780 
RIMTRGTFAN IRLKNQLAPG TEGGFTTNFL NGEVTSIFDA STAYKEAGVP LVVLAGKDYG 

       790        800        810        820        830        840 
MGSSRDWAAK GTFLLGVKAV IAESFERIHR SNLVGMGVLP LQYKNGETAD SLGINGDETF 

       850        860        870        880        890        900 
EFVLPGDLKP RQDVTVKVTG KDGNTRDITV MCRIDTPVEI DYYKNGGILQ TVLRGILSKS 


QGEVKA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	"Protein recycling is a major component of post-irradiation recovery in Deinococcus radiodurans strain R1." Joshi B.S., Schmid R., Altendorf K., Apte S.K. Biochem. Biophys. Res. Commun. 320:1112-1117(2004) [PubMed: 15249204] [Abstract] Cited for: PROTEIN SEQUENCE OF 3-19. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF11276.1.
PIR	G75362.
RefSeq	NP_295443.1. NC_001263.1.
3D structure databases
HSSP	HSSP built from PDB template 2B3Y based on UniProtKB P21399.
ProteinModelPortal	Q9RTN7.
SMR	Q9RTN7. Positions 7-897.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1799543.
GenomeReviews	Gene locus DR_1720 in contig AE000513_GR.
KEGG	dra:DR_1720.
NMPDR	fig\|243230.1.peg.1902.
PATRIC	21631072. VBIDeiRad64572_1931.
TIGR	DR_1720.
Phylogenomic databases
HOGENOM	HBG289738.
OMA	FGIVHQV.
PhylomeDB	Q9RTN7.
ProtClustDB	PRK09277.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1720-MONOMER.
Family and domain databases
InterPro	IPR015931. 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]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KO	K01681.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01341. Aconitase_1. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACON_DEIRA

Accession

Primary (citable) accession number: Q9RTN7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents