Q8NQ98 (ACON_CORGL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aconitate hydratase
EC=4.2.1.3

Gene names

Name:	acn
Ordered Locus Names:	Cgl1540, cg1737

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	939 AA.
Sequence status	Complete.
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.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Induction	Repressed by AcnR.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.
Sequence caution	The sequence BAB98933.1 differs from that shown. Reason: Erroneous initiation. The sequence CAF21548.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aconitate hydratase activity Inferred from electronic annotation. Source: EC citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Chain	1 – 939	939	Aconitate hydratase		PRO_0000076657
Sites
	Metal binding	475	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	541	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	544	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	71	1	D → N in BAA76717. Ref.1
	Sequence conflict	122	1	M → V in BAA76717. Ref.1
	Sequence conflict	555	1	I → Y in BAA76717. Ref.1
	Sequence conflict	745	1	N → Y in BAA76717. Ref.1
	Sequence conflict	888	1	T → I in BAA76717. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8NQ98 [UniParc]. Last modified February 7, 2006. Version 2. Checksum: 3488BCA190A07F13	FASTA	939	101,726
	10 20 30 40 50 60 MTESKNSFNA KSTLEVGDKS YDYFALSAVP GMEKLPYSLK VLGENLLRTE DGANITNEHI 70 80 90 100 110 120 EAIANWDASS DPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVAALGGD PNDVNPLNPA 130 140 150 160 170 180 EMVIDHSVIV EAFGRPDALA KNVEIEYERN EERYQFLRWG SESFSNFRVV PPGTGIVHQV 190 200 210 220 230 240 NIEYLARVVF DNEGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP 250 260 270 280 290 300 RVVGFKLTGE IPVGVTATDV VLTITEMLRD HGVVQKFVEF YGSGVKAVPL ANRATIGNMS 310 320 330 340 350 360 PEFGSTCAMF PIDEETTKYL RLTGRPEEQV ALVEAYAKAQ GMWLDEDTVE AEYSEYLELD 370 380 390 400 410 420 LSTVVPSIAG PKRPQDRILL SEAKEQFRKD LPTYTDDAVS VDTSIPATRM VNEGGGQPEG 430 440 450 460 470 480 GVEADNYNAS WAGSGESLAT GAEGRPSKPV TVASPQGGEY TIDHGMVAIA SITSCTNTSN 490 500 510 520 530 540 PSVMIGAGLI ARKAAEKGLK SKPWVKTICA PGSQVVDGYY QRADLWKDLE AMGFYLSGFG 550 560 570 580 590 600 CTTCIGNSGP LPEEISAAIN EHDLTATAVL SGNRNFEGRI SPDVKMNYLA SPIMVIAYAI 610 620 630 640 650 660 AGTMDFDFEN EALGQDQDGN DVFLKDIWPS TEEIEDTIQQ AISRELYEAD YADVFKGDKQ 670 680 690 700 710 720 WQELDVPTGD TFEWDENSTY IRKAPYFDGM PVEPVAVTDI QGARVLAKLG DSVTTDHISP 730 740 750 760 770 780 ASSIKPGTPA AQYLDEHGVE RHDYNSLGSR RGNHEVMMRG TFANIRLQNQ LVDIAGGYTR 790 800 810 820 830 840 DFTQEGAPQA FIYDASVNYK AAGIPLVVLG GKEYGTGSSR DWAAKGTNLL GIRAVITESF 850 860 870 880 890 900 ERIHRSNLIG MGVVPLQFPA GESHESLGLD GTETFDITGL TALNEGETPK TVKVTATKEN 910 920 930 GDVVEFDAVV RIDTPGEADY YRHGGILQYV LRQMAASSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Brevibacterium lactofermentum ATCC 13869 acn gene for aconitase." Nakamura J., Kimura E., Oosumi T., Matsui K., Nakamatsu T. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13869 / DSMZ 1412 / NCIMB 9567.
[2]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB025424 Genomic DNA. Translation: BAA76717.1. BA000036 Genomic DNA. Translation: BAB98933.1. Different initiation. BX927152 Genomic DNA. Translation: CAF21548.1. Different initiation.
RefSeq	NP_600755.1. NC_003450.3. YP_225824.1. NC_006958.1.
3D structure databases
ModBase	Search...
2D gel databases
World-2DPAGE	0001:Q8NQ98.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019512. 3344469.
GenomeReviews	Gene locus Cgl1540 in contig BA000036_GR. Gene locus cg1737 in contig BX927147_GR.
KEGG	cgb:cg1737. cgl:NCgl1482.
PATRIC	21495127. VBICorGlu203724_1507.
Phylogenomic databases
HOGENOM	HBG289738.
OMA	YSKAQGM.
PhylomeDB	Q8NQ98.
ProtClustDB	PRK09277.
Enzyme and pathway databases
BioCyc	CGLU196627:CG1737-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. 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. 3 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. 2 hits. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACON_CORGL

Accession

Primary (citable) accession number: Q8NQ98
Secondary accession number(s): Q6M550, Q9WXJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 7, 2006
Last modified:	January 25, 2012
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program