Q0BZK2 (HUTH_HYPNA) 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:	HNE_2396

Organism

Hyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]

Taxonomic identifier

228405 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Hyphomonas

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-histidine = urocanate + NH3. 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
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	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 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 513	513	Histidine ammonia-lyase HAMAP MF_00229		PRO_0000336584
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)
	Q0BZK2 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: B19CE609D7BA30CF	FASTA	513	53,768
	10 20 30 40 50 60 MTTITLTPGS VPLSSWRALW QGATPKLDPA CRPTIAGSAS AVARILSRGK PVYGINTGFG 70 80 90 100 110 120 KLAAVRIPDD QLEMLQRNIV LSHAAGVGEP SPANIVRLMM ALKMTNLGRG ASGVRLETID 130 140 150 160 170 180 LMEAMLAADL LPLIPAQGSV GASGDLAPLA HMACAMIGVG DVFLKGERLS AASAFRKAGL 190 200 210 220 230 240 TPLPALAAKE GLALLNGTQF STACALAGLF EAERILQSAL VTGALSTEAA KGSDAPFDPR 250 260 270 280 290 300 IHELRGHRGQ IDCADILRDL MAGSAIRASH LENDTRVQDP YCIRCQPQVA GAALTLLRQA 310 320 330 340 350 360 ADTLLTESNG VSDNPLIFPE TDEALSGGNF HAEPVAFAAD MIAMALCEIG SISERRIAML 370 380 390 400 410 420 VDPALSGMPA FLTPQPGLNS GFMIPQVTAA ALVSENKQMA FPASVDSIPT SANQEDHVSM 430 440 450 460 470 480 AAHGARRLLT MAKNVDYILG IELLAAAQAC DFHAPLRSSD ALEALRARIR QDVPPLDHDR 490 500 510 LMHPDIEAAT GLIRSGEAIR AVNRPLPALE AAP

References

[1]

"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus." Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L. J. Bacteriol. 188:6841-6850(2006) [PubMed: 16980487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15444.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000158 Genomic DNA. Translation: ABI76153.1.
RefSeq	YP_761091.1. NC_008358.1.
3D structure databases
ProteinModelPortal	Q0BZK2.
SMR	Q0BZK2. Positions 2-504.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0BZK2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4287124.
GenomeReviews	Gene locus HNE_2396 in contig CP000158_GR.
KEGG	hne:HNE_2396.
NMPDR	fig|228405.5.peg.2310.
PATRIC	32217643. VBIHypNep17450_2404.
TIGR	HNE_2396.
Phylogenomic databases
eggNOG	COG2986.
HOGENOM	HBG510887.
OMA	MSERRTE.
ProtClustDB	PRK09367.
Enzyme and pathway databases
BioCyc	HNEP81032:HNE_2396-MONOMER.
Family and domain databases
HAMAP	MF_00229. His_ammonia-lyase. [Tree]
InterPro	IPR005921. HutH. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. 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	K01745.
Pfam	PF00221. PAL. 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_HYPNA

Accession

Primary (citable) accession number: Q0BZK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program