ID HUTH_CAEEL Reviewed; 677 AA. AC Q20502; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 58. DE RecName: Full=Probable histidine ammonia-lyase; DE Short=Histidase; DE EC=4.3.1.3; GN ORFNames=F47B10.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; 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 RT investigating biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: L-histidine = urocanate + NH(3). CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L- CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. CC -!- INTERACTION: CC Q9TZ38:gei-4; NbExp=1; IntAct=EBI-322047, EBI-329192; CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), CC which is formed autocatalytically by cyclization and dehydration CC of residues Cys-Ser-Gly (By similarity). CC -!- SIMILARITY: Belongs to the PAL/histidase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z68004; CAA91982.1; -; Genomic_DNA. DR PIR; T22333; T22333. DR RefSeq; NP_509820.1; -. DR UniGene; Cel.9060; -. DR HSSP; P21310; 1GKM. DR DIP; DIP:27218N; -. DR IntAct; Q20502; 2. DR Ensembl; F47B10.2; Caenorhabditis elegans. DR GeneID; 181279; -. DR KEGG; cel:F47B10.2; -. DR NMPDR; fig|6239.3.peg.24527; -. DR WormBase; WBGene00009813; F47B10.2. DR WormPep; F47B10.2; CE03352. DR OMA; Q20502; HCTAASL. DR BRENDA; 4.3.1.3; 672. DR NextBio; 913256; -. DR ArrayExpress; Q20502; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016211; F:ammonia ligase activity; IEA:InterPro. DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006548; P:histidine catabolic process; IEA:InterPro. DR InterPro; IPR005921; HutH. DR InterPro; IPR001106; Phe/His_NH3-lyase. DR Pfam; PF00221; PAL; 1. DR TIGRFAMs; TIGR01225; hutH; 1. DR PROSITE; PS00488; PAL_HISTIDASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Histidine metabolism; Lyase. FT CHAIN 1 677 Probable histidine ammonia-lyase. FT /FTId=PRO_0000161061. FT MOD_RES 270 270 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 269 271 5-imidazolinone (Cys-Gly) (By FT similarity). 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 //