ID   HUTH_MARMM              Reviewed;         507 AA.
AC   Q0AP92;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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=Mmar10_1603;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
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; CP000449; ABI65895.1; -; Genomic_DNA.
DR   RefSeq; YP_756833.1; -.
DR   GeneID; 4283925; -.
DR   GenomeReviews; CP000449_GR; Mmar10_1603.
DR   KEGG; mmr:Mmar10_1603; -.
DR   NMPDR; fig|394221.5.peg.1566; -.
DR   HOGENOM; Q0AP92; -.
DR   OMA; Q0AP92; 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_0000336585.
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   507 AA;  52202 MW;  BB3F77F890CA662E CRC64;
     MTTVTIKPGA MVLADWADIW RGATIRIDPE AKAGVDAAAA TVDRLIASGE AVYGLNTGFG
     KLAQTRIADD ELATLQERLV LSHAAGIGEA LDSRIVRLVM ALKLASLGRG ASGVRWTTIA
     AMQALLDADV LPVIPSQGSV GASGDLAPLA HMSAALIGAG EATWQGQRMP ASDALAKAGL
     KPVQLGPKEG LALLNGTQTS TALALAGLFE VEAGFQAALV SGALSVDAAK GSVAPFDPRI
     HSLRGHPGQI DVAAALRGLL DGSGILSSHE GCEKIQDPYC LRCQPQVMGA VLDLLRQAGA
     VLEREANAVT DNPLIFTDTD EAISGGNFHA EPVAFAADQI AMAACEIGSI CERRIALLTD
     PAVSGLPAFL TPNPGINSGF MIAHVTAAAL VSENKQKAYP ASVDSIPTSA NQEDHVSMAT
     HGAFRLLKMA ENLHVVVGIE LLCGAQGTDF HAGLTSSPTL ETAKATLRKQ VPAYGDDRYF
     ATDIANARDL VTGRGLVADA GTLPGIA
//