ID HUTH_BURCM Reviewed; 507 AA. AC Q0BDK6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Histidine ammonia-lyase; DE Short=Histidase; DE EC=4.3.1.3; GN Name=hutH; OrderedLocusNames=Bamb_2211; OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia OS cepacia (strain AMMD)). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=339670; 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., Pitluck S., Bruce D., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., RA Konstantinidis K., Ramette A., Tiedje J., Richardson P.; RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."; RL Submitted (AUG-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; CP000440; ABI87767.1; -; Genomic_DNA. DR RefSeq; YP_774101.1; -. DR GeneID; 4310117; -. DR GenomeReviews; CP000440_GR; Bamb_2211. DR KEGG; bam:Bamb_2211; -. DR NMPDR; fig|339670.3.peg.3796; -. DR OMA; Q0BDK6; FAPDIEA. 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 1 507 Histidine ammonia-lyase. FT /FTId=PRO_1000021549. FT MOD_RES 142 142 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 141 143 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 507 AA; 53309 MW; 77E97E1B72B5549B CRC64; MITLTPGHLT LPQLRKIARE SVQLTLDPAS FAKIDAGAKA VADIAAKGEP AYGINTGFGR LASTHIPHDQ LELLQKNLVL SHAVGVGEPM ARSSVRLLMA LKLSSLGRGH SGIRREVMDA LITLFNADVL PLIPVKGSVG ASGDLAPLAH MSAVLLGVGE VFIRGERASA LDGLRVAGLA PLTLQAKEGL ALLNGTQAST ALALDNMFSI EDLYRTALVA GALSVDAAAG SVKPFDARIH ELRGHRGQID AAAAYRDLLD GSPINQSHRD CDKVQDPYSL RCQPQVMGAC LDQMRHAADV LLIEANAVSD NPLIFPDTGE VLSGGNFHAE PVAFAADNLA LAAAEIGALA ERRIALLIDA TLSGLPPFLV KDGGVNSGFM IAHVTAAALA SENKTLAHPA SVDSLPTSAN QEDHVSMATF AARKLADIAD NTKYILAIEL LAAAQGVDLR APYHTSPKLA PVMETIRGHV AHYELDHYFA PDIAVIAKLV SERAFAKVAP FSFASEQ //