ID   HUTH_STRGR              Reviewed;         514 AA.
AC   P24221;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Histidine ammonia-lyase;
DE            Short=Histidase;
DE            EC=4.3.1.3;
GN   Name=hutH;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23345 / DSM 40236 / JCM 4644 / NBRC 12875 / NCIMB 13023 / NRRL
RC   B-2682 / VKM Ac-800 / IMRU 3463;
RX   PubMed=1537807; DOI=10.1128/jb.174.5.1647-1655.1992;
RA   Wu P.-C., Kroening T.A., White P.J., Kendrick K.E.;
RT   "Purification of histidase from Streptomyces griseus and nucleotide
RT   sequence of the hutH structural gene.";
RL   J. Bacteriol. 174:1647-1655(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1612436; DOI=10.1016/0378-1119(92)90535-w;
RA   Wu P.-C., Kroening T.A., White P.J., Kendrick K.E.;
RT   "Histidine ammonia-lyase from Streptomyces griseus.";
RL   Gene 115:19-25(1992).
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   -!- 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 {ECO:0000305}.
CC   -!- INDUCTION: By histidine.
CC   -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC       is formed autocatalytically by cyclization and dehydration of residues
CC       Cys-Ser-Gly. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M77841; AAA26769.1; ALT_INIT; Genomic_DNA.
DR   PIR; JC1172; JC1172.
DR   AlphaFoldDB; P24221; -.
DR   SMR; P24221; -.
DR   STRING; 1911.GCA_001715295_02093; -.
DR   SABIO-RK; P24221; -.
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   2: Evidence at transcript level;
KW   Cytoplasm; Histidine metabolism; Lyase.
FT   CHAIN           1..514
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161038"
FT   MOD_RES         144
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        143..145
FT                   /note="5-imidazolinone (Cys-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   514 AA;  53111 MW;  83559BE9FA9A3BB4 CRC64;
     MHTVVVGTSG TTAEDVVAVA RHGARVELSA AAVEALAAAR LIVDALAAKP EPVYGVSTGF
     GALASRHIGT ELRAQLQRNI VRSHAAGMGP RVEREVVRAL MFLRLKTVAS GHTGVRPEVA
     QTMADVLNAG ITPVVHEYGS LGCSGDLAPL SHCALTLMGE GEAEGPDGTV RPAGELLAAH
     GIAPVELREK EGLALLNGTD GMLGMLVMAL ADLRNLYTSA DITAALSLEA LLGTDKVLAP
     ELHAIRPHPG QGVSADNMSR VLAGSGLTGH HQDDAPRVQD AYSVRCAPQV NGAGRDTLDH
     AALVAGRELA SSVDNPVVLP DGRVESNGNF HGAPVAYVLD FLAIVAADLG SICERRTDRL
     LDKNRSHGLP PFLADDAGVD SGLMIAQYTQ AALVSEMKRL AVPASADSIP SSAMQEDHVS
     MGWSAARKLR TAVDNLARIV AVELYAATRA IELRAAEGLT PAPASEAVVA ALRAAGAEGP
     GPDRFLAPDL AAADTFVREG RLVAAVEPVT GPLA