ID   HUTH_AGRRH              Reviewed;         511 AA.
AC   Q9KWE4;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000255|HAMAP-Rule:MF_00229};
DE            Short=Histidase {ECO:0000255|HAMAP-Rule:MF_00229};
DE            EC=4.3.1.3 {ECO:0000255|HAMAP-Rule:MF_00229};
GN   Name=hutH {ECO:0000255|HAMAP-Rule:MF_00229}; ORFNames=riorf40;
OS   Agrobacterium rhizogenes.
OG   Plasmid pRi1724.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MAFF03-01724;
RX   PubMed=10907845; DOI=10.1093/dnares/7.3.157;
RA   Moriguchi K., Maeda Y., Satou M., Kataoka M., Tanaka N., Yoshida K.;
RT   "Analysis of unique variable region of a plant root inducing plasmid,
RT   pRi1724, by the construction of its physical map and library.";
RL   DNA Res. 7:157-163(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MAFF03-01724;
RX   PubMed=11273700; DOI=10.1006/jmbi.2001.4488;
RA   Moriguchi K., Maeda Y., Satou M., Hardayani N.S.N., Kataoka M., Tanaka N.,
RA   Yoshida K.;
RT   "The complete nucleotide sequence of a plant root-inducing (Ri) plasmid
RT   indicates its chimeric structure and evolutionary relationship between
RT   tumor-inducing (Ti) and symbiotic (Sym) plasmids in Rhizobiaceae.";
RL   J. Mol. Biol. 307:771-784(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232,
CC         ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00229};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00229}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00229}.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Ala-Ser-Gly. {ECO:0000255|HAMAP-Rule:MF_00229}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00229}.
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DR   EMBL; AB039932; BAA97751.1; -; Genomic_DNA.
DR   EMBL; AP002086; BAB16159.1; -; Genomic_DNA.
DR   RefSeq; NP_066621.1; NC_002575.1.
DR   RefSeq; WP_010900230.1; NC_002575.1.
DR   AlphaFoldDB; Q9KWE4; -.
DR   SMR; Q9KWE4; -.
DR   UniPathway; UPA00379; UER00549.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00229; His_ammonia_lyase; 1.
DR   InterPro; IPR001106; Aromatic_Lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR005921; HutH.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   PANTHER; PTHR10362; PTHR10362; 1.
DR   Pfam; PF00221; Lyase_aromatic; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR01225; hutH; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Histidine metabolism; Lyase; Plasmid.
FT   CHAIN           1..511
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000160982"
FT   MOD_RES         143
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        142..144
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   511 AA;  52877 MW;  B3C88D419EF74B53 CRC64;
     MTIVLRPGSV PLHHLADIYW NNGSAKLDPS FDAAVLKGAA RIAEIAAGNA PVYGINTGFG
     KLASIKIDAA DLATLQRNLI LSHCCGVGAP LPENVVRLIM ALKLISLGRG ASGVRIELIR
     LIEGMLEKGV IPVIPEKGSV GASGDLAPLA HMSATMMGEG EAFYQGVQMP SKDALAKAGL
     SPVVLAAKEG LALINGTQTS TALALAGLFR AHRAAQSALV TGALSTDAAM GSSAPFHPDI
     HTLRGHKGQI DAGSALRNLL QGSEIRESHI EGDERVQDPY CIRCQPQVDG ACLDLLASVA
     RTLEIEANAV TDNPLVLSDN SVVSGGNFHA EPVAFAADQT ALAVCEIGAI AQRRIALLVD
     PALSYGLPAF LSKKPGLNSG LMIAEVTSAA LMSENKQMSH PASVDSTPTS ANQEDHVSMA
     CHGARRLLAM TDNLFGILGI EALAAVQGVE LRGPLKTSPE LEKAAAVLRS AVPVLEDDRY
     MATDLKAAIE VVASGALVSA ISSGILPVLE A