ID HUTH_MESSB Reviewed; 511 AA. AC Q11E18; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Histidine ammonia-lyase; DE Short=Histidase; DE EC=4.3.1.3; GN Name=hutH; OrderedLocusNames=Meso_2985; OS Mesorhizobium sp. (strain BNC1). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=266779; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Richardson P.; RT "Complete sequence of chromosome of Mesorhizobium sp. BNC1."; RL Submitted (JUN-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; CP000390; ABG64357.1; -; Genomic_DNA. DR RefSeq; YP_675522.1; -. DR GeneID; 4181421; -. DR GenomeReviews; CP000390_GR; Meso_2985. DR KEGG; mes:Meso_2985; -. DR NMPDR; fig|266779.1.peg.1513; -. DR HOGENOM; Q11E18; -. DR OMA; Q11E18; AHMAAVM. DR BioCyc; MSP266779:MESO_2985-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 1 511 Histidine ammonia-lyase. FT /FTId=PRO_1000021560. FT MOD_RES 143 143 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 142 144 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 511 AA; 53243 MW; B80D982815C6102C CRC64; MTIILHPGSV LLRDLATIYW TGVPARLDPS FDAGIVKAAD RIAEIAAGNA PVYGINTGFG KLASIKIDSA DVAALQRNLV LSHCCGVGEA LPENVVRLMM ALKLVSLGRG ASGVRLELVR LIEAMLARGV IPVIPEKGSV GASGDLAPLA HMAAVMMGHG EAFFGGERLN GATALLKAGL QPVELAAKEG LALINGTQTS TALALAGLFR AHRAAQSALI TGAMSTDAAM GSSAPFHPEI HTLRGHRGQI DTAEALRALL ENSPIRQSHI EGDERVQDPY CIRCQPQVDG ACLDLLRSVA RTLEIEANAV TDNPLVLSDN SVVAGGNFHA EPVAFAADQI VLAICEIGAI AQRRIALLVD PALSYGLPAF LAKKPGLNSG LMIAEVTSAA LMSENKQMSH PASVDSTPTS ANQEDHVSMA CHGARRLLPM TENLFAIIGI EALCAAQGVE LRAPLATSPE LTKAIAAIRN VVPSLEEDRY MANDLKAATV LIASGSLNES VSSGILPALE V //