ID HUTH_ANADE Reviewed; 508 AA. AC Q2IIV4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 27. DE RecName: Full=Histidine ammonia-lyase; DE Short=Histidase; DE EC=4.3.1.3; GN Name=hutH; OrderedLocusNames=Adeh_1814; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), CC which is formed autocatalytically by cyclization and dehydration CC of residues Ala-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; CP000251; ABC81586.1; -; Genomic_DNA. DR RefSeq; YP_465023.1; -. DR GeneID; 3887396; -. DR GenomeReviews; CP000251_GR; Adeh_1814. DR KEGG; ade:Adeh_1814; -. DR HOGENOM; Q2IIV4; -. DR OMA; Q2IIV4; FAPDIEA. DR BioCyc; ADEH290397:ADEH_1814-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016211; F:ammonia ligase activity; IEA:InterPro. DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:HAMAP. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006548; P:histidine catabolic process; IEA:HAMAP. DR HAMAP; MF_00229; -; 1. 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 3: Inferred from homology; KW Complete proteome; Cytoplasm; Histidine metabolism; Lyase. FT CHAIN 1 508 Histidine ammonia-lyase. FT /FTId=PRO_0000336582. FT MOD_RES 144 144 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 143 145 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 508 AA; 53101 MW; 52FF0095D52F0AD5 CRC64; METLLLDGET LTLEQVRAVA TGAARAALAP AARERVRRSR ALVDARLEDG EAHYGINTGF GTLAEVRIPR ADLERLQRNL VLSHAAGVGA PLPLAEARAL VLLRANVLAK GVSGIRERTL ELLLAMLERG VVPVVPERGS VGASGDLAPL AHLALVLIGD GEAFLAPPGA AAPPERLPGG EALRRAGLEP VVLQPKEGLA LVNGTQAMAA VGTLALLRAE RLAALADLAG AMTLEGLLGS HRPFAPEIQA ARGQPGQIEA AAHLRALLAG SELNASHQGP GCHKVQDPYS LRCMPQVHGA ARDGIGFCRG VLAREVNAAT DNPLVFPDTG EIVSGGNFHG QPVALALDVL AVAASHLAAI SERRVEQLVN PSLSGLPPFL APQHGLNSGF MIAQVTSAAL VSENKVLCHP ASVDSIPSSA GREDHVSMGM TAALKARQVV ENVRTCLAIE LLVAAQALDL RAPLRPAQRV ADAHARLRER VPHLSEDRAL YRDIEAVSRL VDEGALEL //