ID HUTH_PSYCK Reviewed; 520 AA. AC Q1Q9E4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 25. DE RecName: Full=Histidine ammonia-lyase; DE Short=Histidase; DE EC=4.3.1.3; GN Name=hutH; OrderedLocusNames=Pcryo_1932; OS Psychrobacter cryohalolentis (strain K5). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=335284; 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., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5."; RL Submitted (MAR-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; CP000323; ABE75709.1; -; Genomic_DNA. DR RefSeq; YP_581193.1; -. DR GeneID; 4034669; -. DR GenomeReviews; CP000323_GR; Pcryo_1932. DR KEGG; pcr:Pcryo_1932; -. DR NMPDR; fig|335284.3.peg.2412; -. DR HOGENOM; Q1Q9E4; -. DR OMA; Q1Q9E4; FAPDIEA. DR BioCyc; PCRY335284:PCRYO_1932-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 1 520 Histidine ammonia-lyase. FT /FTId=PRO_1000021567. FT MOD_RES 147 147 2,3-didehydroalanine (Ser) (By FT similarity). FT CROSSLNK 146 148 5-imidazolinone (Ala-Gly) (By FT similarity). SQ SEQUENCE 520 AA; 55756 MW; 1FD92E53A3EEF57E CRC64; MTAIKKLTLQ PRQLSFEILR DIYEQPVILT LPDSAYEAID ASHEDVQTII RRDKSAYGIN TGFGLLAKTR ISDDQLELLQ RNLIVSHSVG TGEALPANVV RLIMVMKVTS LAQGVSGVRR AVVDSLLGLI NNQITPNIPA KGSVGASGDL APLSHMTLAM MGEGHVYVDG NKVLAADALA QHGLEPITLA AKEGLALING TQVSTALALR GYFLARDLLE TATIVGSLSI DAAKGSDAPF DARIHEVRGH HGQIEIAKAH RQLIKGSAIR ASHDGEQDDR VQDPYCLRCQ PQVMGACLDI INQAGKTLLI ESNAVTDNPL IFNNEDGPVA ISGGNFHAEP VAFAADILAL AIAEIGSMSE RRIALLIDAT LSGGLPPFLV DNAGVNSGFM IAHVTAAALA SENKSIAHPG SVDSIPTSAN QEDHVSMATY CARRLYEMAQ NTATIIGIEL LAAGQGIDFH RGLETSEPLT MAHQKLREQV TFYDKDRYLA PDIEAAKQLV LDGTLAEHWQ PLRSNWYDSK //