Q8FVB4 (HUTH_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine ammonia-lyase
Short name=Histidase
EC=4.3.1.3

Gene names

Name:	hutH
Ordered Locus Names:	BRA0930, BS1330_II0922

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidine = urocanate + NH3. HAMAP-Rule MF_00229
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. HAMAP-Rule MF_00229
Subcellular location	Cytoplasm Potential HAMAP-Rule 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-Rule MF_00229
Sequence similarities	Belongs to the PAL/histidase family.

Ontologies

Keywords
Biological process	Histidine metabolism
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Complete proteome
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: UniProtKB-UniPathway histidine catabolic process to glutamate and formate Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histidine ammonia-lyase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	Histidine ammonia-lyase HAMAP-Rule MF_00229		PRO_0000160996
Amino acid modifications
	Modified residue	143	1	2,3-didehydroalanine (Ser) By similarity
	Cross-link	142 ↔ 144		5-imidazolinone (Ala-Gly) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8FVB4 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 734B242E8D8478F5	FASTA	511	53,340
	10 20 30 40 50 60 MTIILKPGSV PLETLEKIYR EGLPVRIDPA FHAGIEKAAA RIAEIAAGDA PVYGINTGFG 70 80 90 100 110 120 KLASIRIAAG DVATLQRNLI LSHCCGVGEP LSENIVRLIM ALKLVSLGRG ASGVRLEVIT 130 140 150 160 170 180 LIEAMLEKGV IPMIPEKGSV GASGDLAPLA HMTAAMIGEG EAFYRGERLS GAKALGKAGL 190 200 210 220 230 240 KPVVLAAKEG LALINGTQTS TALALAGLFR AHRAVRTALI TGALSTDAAM GSDAPFHEEI 250 260 270 280 290 300 HQLRGHKGQI DAGRALRTLL EGSAIRRSHL EGDQRVQDPY CIRCQPQVDG ACLDILRQAA 310 320 330 340 350 360 RTLEIEANAV TDNPLVLSDG RAVSGGNFHA EPVAFAADQI ALAVCEIGAI SQRRIALLVD 370 380 390 400 410 420 PSLSFGLPAF LTRKPGLNSG LMIAEVTSAA LMSENKQMAH PASVDSTPTS ANQEDHVSMA 430 440 450 460 470 480 CHGARRLLQM TANLNAIIGI EALTGALGVE LRKPLTTSAE LAKVIAALRA KVVTLEEDRY 490 500 510 MADDLKAAAE LVADGTLSGV ISAGILPDLE A

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014292 Genomic DNA. Translation: AAN34102.1. CP002998 Genomic DNA. Translation: AEM20378.1.
RefSeq	NP_700097.1. NC_004311.2. YP_005614604.1. NC_017250.1.
3D structure databases
ProteinModelPortal	Q8FVB4.
SMR	Q8FVB4. Positions 2-509.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BRA0930.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN34102; AAN34102; BRA0930. AEM20378; AEM20378; BS1330_II0922.
GeneID	1165374. 12139153.
KEGG	bms:BRA0930. bsi:BS1330_II0922.
PATRIC	17794679. VBIBruSui107850_3148.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2986.
HOGENOM	HOG000237619.
KO	K01745.
OMA	NAPVYGI.
ProtClustDB	PRK09367.
Enzyme and pathway databases
UniPathway	UPA00379; UER00549.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
HAMAP	MF_00229. His_ammonia-lyase.
InterPro	IPR001106. Aromatic_Lyase. IPR024083. Fumarase/histidase_N. IPR005921. HutH. IPR008948. L-Aspartase-like. IPR022313. Phe/His_NH3-lyase_AS. [Graphical view]
Pfam	PF00221. Lyase_aromatic. 1 hit. [Graphical view]
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR01225. hutH. 1 hit.
PROSITE	PS00488. PAL_HISTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HUTH_BRUSU

Accession

Primary (citable) accession number: Q8FVB4
Secondary accession number(s): G0KDU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program