ID   HUTH_STRCO              Reviewed;         512 AA.
AC   Q9EWW1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 115.
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}; OrderedLocusNames=SCO4932;
GN   ORFNames=SCK13.24;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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       Cys-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; AL939121; CAD30922.1; -; Genomic_DNA.
DR   RefSeq; NP_629085.1; NC_003888.3.
DR   RefSeq; WP_003974041.1; NZ_VNID01000027.1.
DR   AlphaFoldDB; Q9EWW1; -.
DR   SMR; Q9EWW1; -.
DR   STRING; 100226.SCO4932; -.
DR   PRIDE; Q9EWW1; -.
DR   GeneID; 1100373; -.
DR   KEGG; sco:SCO4932; -.
DR   PATRIC; fig|100226.15.peg.5011; -.
DR   eggNOG; COG2986; Bacteria.
DR   HOGENOM; CLU_014801_4_1_11; -.
DR   InParanoid; Q9EWW1; -.
DR   OMA; CAPQVAG; -.
DR   PhylomeDB; Q9EWW1; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..512
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000161037"
FT   MOD_RES         144
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT   CROSSLNK        143..145
FT                   /note="5-imidazolinone (Cys-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  52776 MW;  C44CBEED6BB49231 CRC64;
     MHTVVVGTSG VTASDVLAVA RAGARIELSE EAVAALAAAR SVVDALAAKP DPVYGVSTGF
     GALATRHISP ELRGRLQRNI VRSHAAGMGP RVEREVVRAL MFLRLKTVCS GRTGVRPEVA
     QTMADVLNAG ITPVVHEYGS LGCSGDLAPL SHCALTLMGE GDAEGPDGTV RPAGELLAAH
     GIAPVELREK EGLALLNGTD GMLGMLVMAL ADLDTLYKSA DITAALTMEA LLGTDRVLAP
     ELHAIRPHPG QAASAANMAA VLKGSGLTGH HQDDAPRVQD AYSVRCAPQV AGAGRDTMAH
     AGLVAERELA AAVDNPVVLP DGRVESNGNF HGAPVAYVLD FLAVAVADLG SIAERRTDRL
     LDKNRSHGLP PFLADDAGVD SGLMIAQYTQ AALVGELKRL AVPASADSIP SSAMQEDHVS
     MGWSAARKLR TAVDNLARVI AVELYAATRA IQLREGLTPA PASQAVVEAV RAAGVEGPGP
     DRHLAPDLAA ADAFVRAGHL VAAAESVTGP LR