Q5R023 (Q5R023_IDILO) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Aconitate hydratase 2 PIRNR PIRNR036687
EC=4.2.1.3 PIRNR PIRNR036687

Gene names

Name:	acnB EMBL AAV81311.1
Ordered Locus Names:	IL0468 EMBL AAV81311.1

Organism

Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP] EMBL AAV81311.1

Taxonomic identifier

283942 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina › Idiomarina loihiensis

Protein attributes

Sequence length	862 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Citrate = isocitrate. PIRNR PIRNR036687
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. SAAS SAAS015931
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle. PIRNR PIRNR036687
Sequence similarities	Belongs to the aconitase/IPM isomerase family. PIRNR PIRNR036687

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle PIRNR PIRNR036687
Ligand	4Fe-4S SAAS SAAS015931 Iron Iron-sulfur Metal-binding
Molecular function	Lyase PIRNR PIRNR036687 SAAS SAAS015931
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from electronic annotation. Source: InterPro
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 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...

Sequences

	Sequence		Length	Mass (Da)
	Q5R023 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 92BA043E9D40ED82	FASTA	862	94,061
	10 20 30 40 50 60 MLKEYRQHVE ERAAEGIPPK PLNAEQVADL VELLKNPPAG EEDFLVELLA ERVPPGVDEA 70 80 90 100 110 120 AYVKAGFLSA VVKGEIESPV VSKEYAVKLL GNMHGGYNIV TLVELLDDSQ LAELAAKELK 130 140 150 160 170 180 ETILMFDAFH DVEEKMKAGN ALAKEVVESW ANAEWFTNSD ELAKSIKATV FKVTGETNTD 190 200 210 220 230 240 DLSPAPDAWS RPDIPLHAKA MYKMPREGIT DAGKQIEELK EKGHPVAFVG DVVGTGSSRK 250 260 270 280 290 300 SATNSVLWNI GEDMPGTPNK RAGGICIGSK VAPIFFNTMK DAGALVFEAD VEKMNMGDVI 310 320 330 340 350 360 TIYPYEGKIE NEAGEIIAEY DYASRVILDE VRAGGRINLI IGRGLTEKAR ESLGMGPSDL 370 380 390 400 410 420 FRKPEQPADS GKGFSLAQKL VGKACGMEGV RPGAYCEPKM TTVGSQDTTG PMTRDELKDL 430 440 450 460 470 480 ACLGFNSDLV MQSFCHTAAY PKPVDVETQH TLPDFIMNRG GVSLRPGDGI IHSWLNRMLL 490 500 510 520 530 540 PDTVGTGGDS HTRFPLGISF PAGSGLVAFA AATGVMPLDM PESVLVRFKG EMQPGITLRD 550 560 570 580 590 600 LVHAIPAFAI KEGHLTVDKR GKKNIFSGRI LEIEGLDHLT VEQAFELSDA SAERSAAGCT 610 620 630 640 650 660 IDLSEESVAE YLRSNITMLR WMINEGYGDA RTLERRARKM EEWLENPQLT RADKDADYST 670 680 690 700 710 720 VIEIDLNDIK EPIVCCPNDP DDAKFLSEVS GNNVDEVFIG SCMTNIGHFR AAGKLLEKNS 730 740 750 760 770 780 DPLNTRLWIA PPTKMDKAQL EVEGYYDIYE RNGVRTEMPG CSLCMGNQAR VEPGATVLST 790 800 810 820 830 840 STRNFPNRLG DGANVYLTSA ELAAVGAIVG RLPTPEEYLE YAQDINSMAG EVYKYLNFDQ 850 860 MDAFRDAEKA AKENIIPTIN VA

References

[1]

"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy." Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. , Aizawa S., Shibata S., Malahoff A., Alam M. Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017340 Genomic DNA. Translation: AAV81311.1.
RefSeq	YP_154860.1. NC_006512.1.
3D structure databases
ProteinModelPortal	Q5R023.
SMR	Q5R023. Positions 1-850.
ModBase	Search...
Protein-protein interaction databases
STRING	283942.IL0468.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAV81311; AAV81311; IL0468.
GeneID	3172348.
KEGG	ilo:IL0468.
PATRIC	22138957. VBIIdiLoi21852_0470.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000205991.
KO	K01682.
OMA	NVFNGRI.
ProtClustDB	PRK09238.
Enzyme and pathway databases
BioCyc	ILOI283942:GI0U-510-MONOMER.
UniPathway	UPA00223.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR004406. Aconitase_B_bac. IPR015930. Aconitase_B_FeS-bd_bac. IPR015933. Aconitase_B_HEAT-like_bac. IPR015929. Aconitase_B_N_bac. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF3. PTHR11670:SF3. 1 hit.
Pfam	PF00330. Aconitase. 2 hits. PF06434. Aconitase_2_N. 1 hit. PF11791. Aconitase_B_N. 1 hit. [Graphical view]
PIRSF	PIRSF036687. AcnB. 1 hit.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF74778. Aconitase_B_HEAT-like_bac. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR00117. acnB. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q5R023_IDILO

Accession

Primary (citable) accession number: Q5R023

Entry history

Integrated into UniProtKB/TrEMBL:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)