Bifunctional imidazolonepropionase/histidine ammonia-lyase - Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Bifunctional imidazolonepropionase/histidine ammonia-lyase

Including the following 2 domains:

Imidazolonepropionase
EC=3.5.2.7
Alternative name(s):
Imidazolone-5-propionate hydrolase
Histidine ammonia-lyase
Short name=Histidase
EC=4.3.1.3

Gene names

Name:	hutIH
Ordered Locus Names:	BMEII0368

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	925 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H₂O = N-formimidoyl-L-glutamate + H⁺. HAMAP MF_00229 L-histidine = urocanate + NH₃. HAMAP MF_00229
Cofactor	Binds 1 zinc or iron ion per subunit By similarity. HAMAP MF_00229
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. HAMAP MF_00229 Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
Subcellular location	Cytoplasm Potential HAMAP MF_00229.
Post-translational modification	Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly By similarity. HAMAP MF_00229
Sequence similarities	In the N-terminal section; belongs to the HutI family. In the C-terminal section; belongs to the PAL/histidase family.
Sequence caution	The sequence AAL53610.1 differs from that shown. Reason: Frameshift at position 696.

Ontologies

Keywords
Biological process	Histidine metabolism
Cellular component	Cytoplasm
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro histidine catabolic process to glutamate and formamide Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histidine ammonia-lyase activity Inferred from electronic annotation. Source: EC imidazolonepropionase 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 – 925

925

Bifunctional imidazolonepropionase/histidine ammonia-lyase HAMAP MF_00229

PRO_0000160981

Regions

Region

1 – 414

414

Imidazolonepropionase HAMAP MF_00229

Region

415 – 925

511

Histidine ammonia-lyase HAMAP MF_00229

Sites

Metal binding

73

1

Zinc or iron By similarity

Metal binding

75

1

Zinc or iron By similarity

Metal binding

243

1

Zinc or iron By similarity

Metal binding

318

1

Zinc or iron By similarity

Binding site

82

1

Substrate By similarity

Binding site

95

1

Substrate By similarity

Binding site

145

1

Substrate By similarity

Binding site

178

1

Substrate By similarity

Binding site

246

1

Substrate By similarity

Amino acid modifications

Modified residue

557

1

2,3-didehydroalanine (Ser) By similarity

Cross-link

556 ↔ 558

5-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8YD09 [UniParc].

Last modified May 24, 2005. Version 2.
Checksum: 3D7D858028548835
Show »

FASTA

925

97,849

        10         20         30         40         50         60 
MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPD EYASFEKIDC 

        70         80         90        100        110        120 
GNRLITPGLI DCHTHLVHAG NRAHEFELRL QGATYEEVAR AGGGIVSSVR NLRAASEDDL 

       130        140        150        160        170        180 
VRETLPRLDA LIAEGVTTVE VKSGYGLDRD SEIKSLKAAR RLGEERDVAI RTTFLGAHAL 

       190        200        210        220        230        240 
PPEMNGDKAA YIDRVINDML PAIAEQGLAD AVDGFCEGIA FLPDEIARVF DAAKAHDIPV 

       250        260        270        280        290        300 
KLHADQLSNL HGAALAASYG ALSADHLEYT DADGAAAMAS AGTVAVLLPG AYYFIRETQK 

       310        320        330        340        350        360 
PPVEAFRAAG TKMALATDNN PGTSPLTSLL LTMNMGATLF RMTVEECIAG VTREAARALG 

       370        380        390        400        410        420 
ILDQTGTLEI GKDADLAIWD IERPAELVYR IGFNPLWKRV FKGQIKPHVR MEPFMTIILK 

       430        440        450        460        470        480 
PGSVPLETLE KIYREGLPVR IDPAFHAGIE KAAARIAEIA AGDAPVYGIN TGFGKLASIR 

       490        500        510        520        530        540 
IAAGDVATLQ RNLILSHCCG VGEPLSENIV RLIMALKLVS LGRGASGVQL EVITLIEAML 

       550        560        570        580        590        600 
EKGVIPMIPE KGSVGASGDL APLAHMTAAM IGEGEAFYRG ERLSGAKALG KAGLKPVVLA 

       610        620        630        640        650        660 
AKEGLALING TQTSTALALA GLFRAHRAAR TALITGALST DAAMGSDAPF HEEIHQLRGH 

       670        680        690        700        710        720 
KGQIDAGRAL RTLLEGSAIR RSHLEGDQRV QDPYCXRCQP QVDGACLDIL RQAARTLEIE 

       730        740        750        760        770        780 
ANAVTDNPLV LSDGRAVSGG NFHAEPVAFA ADQIALAVCE IGAISQRRIA LLVDPSLSFG 

       790        800        810        820        830        840 
LPAFLARKPG LNSGLMIAEV TSAALMSENK QMAHPASVDS TPTSANQEDH VSMACHGARR 

       850        860        870        880        890        900 
LLQMTANLNA IIGIEALTGA LGVELRKPLT TSAELAKVIA ALRAKVATLE EDRYMADDLK 

       910        920 
AAAELVADGT LSGVISAGIL PDLEA

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References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis."
DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E.

Overbeek R.
Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008918 Genomic DNA. Translation: AAL53610.1. Frameshift.
PIR	AG3555.
RefSeq	NP_541346.1. NC_003318.1.
3D structure databases
ProteinModelPortal	Q8YD09.
SMR	Q8YD09. Positions 5-404.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1198140.
GenomeReviews	Gene locus BMEII0368 in contig AE008918_GR.
KEGG	bme:BMEII0368.
PATRIC	17800400. VBIBruMel146950_2532.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG365519.
PhylomeDB	Q8YD09.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEII0368-MONOMER.
Family and domain databases
HAMAP	MF_00229. His_ammonia-lyase. Fused. [Tree] MF_00372. HutI. Fused. [Tree]
InterPro	IPR013108. Amidohydro_3. IPR005921. HutH. IPR005920. HutI. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR011059. Metal-dep_hydrolase_composite. IPR001106. Phe/His_NH3-lyase. IPR022313. Phe/His_NH3-lyase_AS. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KO	K01468.
Pfam	PF07969. Amidohydro_3. 1 hit. PF00221. PAL. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit. SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR01225. HutH. 1 hit. TIGR01224. HutI. 1 hit.
PROSITE	PS00488. PAL_HISTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HUTIH_BRUME

Accession

Primary (citable) accession number: Q8YD09

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2005
Last sequence update:	May 24, 2005
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

Relevant documents

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents