HUTH1_CAEEL
ID HUTH1_CAEEL Reviewed; 677 AA.
AC Q20502;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000312|WormBase:F47B10.2};
DE Short=Histidase {ECO:0000250|UniProtKB:P42357};
DE EC=4.3.1.3 {ECO:0000255|PROSITE-ProRule:PRU10122};
GN Name=haly-1 {ECO:0000312|WormBase:F47B10.2};
GN ORFNames=F47B10.2 {ECO:0000312|WormBase:F47B10.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-536.
RX PubMed=21455490; DOI=10.1371/journal.pgen.1002013;
RA Murphy J.T., Bruinsma J.J., Schneider D.L., Collier S., Guthrie J.,
RA Chinwalla A., Robertson J.D., Mardis E.R., Kornfeld K.;
RT "Histidine protects against zinc and nickel toxicity in Caenorhabditis
RT elegans.";
RL PLoS Genet. 7:E1002013-E1002013(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232,
CC ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10122};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC {ECO:0000250|UniProtKB:P21310}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Cys-Ser-Gly. {ECO:0000250|UniProtKB:P21310}.
CC -!- DISRUPTION PHENOTYPE: Defective histidine metabolism resulting in
CC elevated histidine levels and resistance to nickel and zinc toxicity.
CC Additionally, slightly resistant to copper, slightly sensitive to
CC cobalt and iron and substantially sensitive to manganese.
CC {ECO:0000269|PubMed:21455490}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; Z68004; CAA91982.1; -; Genomic_DNA.
DR PIR; T22333; T22333.
DR RefSeq; NP_509820.1; NM_077419.6.
DR AlphaFoldDB; Q20502; -.
DR SMR; Q20502; -.
DR BioGRID; 46190; 13.
DR DIP; DIP-27218N; -.
DR IntAct; Q20502; 3.
DR MINT; Q20502; -.
DR STRING; 6239.F47B10.2; -.
DR iPTMnet; Q20502; -.
DR EPD; Q20502; -.
DR PaxDb; Q20502; -.
DR PeptideAtlas; Q20502; -.
DR EnsemblMetazoa; F47B10.2.1; F47B10.2.1; WBGene00009813.
DR GeneID; 181279; -.
DR KEGG; cel:CELE_F47B10.2; -.
DR UCSC; F47B10.2; c. elegans.
DR CTD; 181279; -.
DR WormBase; F47B10.2; CE03352; WBGene00009813; haly-1.
DR eggNOG; KOG0222; Eukaryota.
DR GeneTree; ENSGT00390000009047; -.
DR HOGENOM; CLU_014801_4_0_1; -.
DR InParanoid; Q20502; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 923557at2759; -.
DR PhylomeDB; Q20502; -.
DR Reactome; R-CEL-70921; Histidine catabolism.
DR SignaLink; Q20502; -.
DR UniPathway; UPA00379; UER00549.
DR PRO; PR:Q20502; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00009813; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0006548; P:histidine catabolic process; IMP:WormBase.
DR GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR GO; GO:1990359; P:stress response to zinc ion; IMP:WormBase.
DR GO; GO:0055069; P:zinc ion homeostasis; IMP:WormBase.
DR CDD; cd00332; PAL-HAL; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR005921; HutH.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01225; hutH; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..677
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161061"
FT MOD_RES 270
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 269..271
FT /note="5-imidazolinone (Cys-Gly)"
FT /evidence="ECO:0000250|UniProtKB:P21310"
FT MUTAGEN 536
FT /note="D->N: In am130; causes strong resistance to nickel
FT and zinc toxicity."
FT /evidence="ECO:0000269|PubMed:21455490"
SQ SEQUENCE 677 AA; 74635 MW; E64CCD5B097AAC4F CRC64;
MRLQVQIGTE CVVVPCKPDD TIHAVAKKSV EKLRRLRPKL PLADDYFEVR RTVGNSLLDP
EDLVSDVLKD SDFIIVAASV EETEDAKEAK KQEEIDNARA EIEKIDNRRR KVSFADSLAP
MVLAPPTKLL ILDGNSLLPE DLVRCEKGEC AIQLSMESED RIRKARTFLE KIASEHRAVY
GVTTGFGTFS NVTIPPEKLK KLQLNLIRSH ATGYGEPLAP NRARMLLALR INILAKGHSG
ISVENIKKMI AAFNAFCVSY VPQQGTVGCS GDLCPLAHLA LGLLGEGKMW SPTTGWQPAD
VVLKKNNLEP LELGPKEGLA LINGTQMVTA LGAYTLERAH NIARQADVIA ALSLDVLKGT
TRAYDPDIHR IRPHRGQNLS ALRLRALLHS EANPSQIAES HRNCTKVQDA YTLRCVPQVH
GVVHDTIEFV REIITTEMNS ATDNPLVFAD REEIISGGNF HGEYPAKALD FLAIAVAELA
QMSERRLERL VNKELSGLPT FLTPDGGLNS GFMTVQLCAA SLVSENKVLC HPSSVDSIPT
SCNQEDHVSM GGFAARKALT VVEHVEAVLA MELLAACQGI EFLKPLISTA PLHKIYQLVR
SVAPPLNEDR YMKPEIDAVL EMIRENRIWE AVLPHLETLE AMEELDPDAL RQFTKTPTGI
VQDRSMIPIS DDEESIE
