ID   HUTH_HYPNA              Reviewed;         513 AA.
AC   Q0BZK2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Histidine ammonia-lyase;
DE            Short=Histidase;
DE            EC=4.3.1.3;
GN   Name=hutH; OrderedLocusNames=HNE_2396;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
RA   Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
RA   Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
RA   Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
RA   Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
RA   Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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.
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DR   EMBL; CP000158; ABI76153.1; -; Genomic_DNA.
DR   RefSeq; YP_761091.1; -.
DR   GeneID; 4287124; -.
DR   GenomeReviews; CP000158_GR; HNE_2396.
DR   KEGG; hne:HNE_2396; -.
DR   NMPDR; fig|228405.5.peg.2310; -.
DR   TIGR; HNE_2396; -.
DR   HOGENOM; Q0BZK2; -.
DR   OMA; Q0BZK2; AHMAAVM.
DR   BioCyc; HNEP81032:HNE_2396-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    513       Histidine ammonia-lyase.
FT                                /FTId=PRO_0000336584.
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   513 AA;  53768 MW;  B19CE609D7BA30CF CRC64;
     MTTITLTPGS VPLSSWRALW QGATPKLDPA CRPTIAGSAS AVARILSRGK PVYGINTGFG
     KLAAVRIPDD QLEMLQRNIV LSHAAGVGEP SPANIVRLMM ALKMTNLGRG ASGVRLETID
     LMEAMLAADL LPLIPAQGSV GASGDLAPLA HMACAMIGVG DVFLKGERLS AASAFRKAGL
     TPLPALAAKE GLALLNGTQF STACALAGLF EAERILQSAL VTGALSTEAA KGSDAPFDPR
     IHELRGHRGQ IDCADILRDL MAGSAIRASH LENDTRVQDP YCIRCQPQVA GAALTLLRQA
     ADTLLTESNG VSDNPLIFPE TDEALSGGNF HAEPVAFAAD MIAMALCEIG SISERRIAML
     VDPALSGMPA FLTPQPGLNS GFMIPQVTAA ALVSENKQMA FPASVDSIPT SANQEDHVSM
     AAHGARRLLT MAKNVDYILG IELLAAAQAC DFHAPLRSSD ALEALRARIR QDVPPLDHDR
     LMHPDIEAAT GLIRSGEAIR AVNRPLPALE AAP
//