HUTH_STRPG
ID HUTH_STRPG Reviewed; 513 AA.
AC A2RGS5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=SpyM51735;
OS Streptococcus pyogenes serotype M5 (strain Manfredo).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=160491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Manfredo;
RX PubMed=17012393; DOI=10.1128/jb.01227-06;
RA Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT "Complete genome of acute rheumatic fever-associated serotype M5
RT Streptococcus pyogenes strain Manfredo.";
RL J. Bacteriol. 189:1473-1477(2007).
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; AM295007; CAM31057.1; -; Genomic_DNA.
DR RefSeq; WP_011889213.1; NC_009332.1.
DR AlphaFoldDB; A2RGS5; -.
DR SMR; A2RGS5; -.
DR PRIDE; A2RGS5; -.
DR KEGG; spf:SpyM51735; -.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OMA; CAPQVAG; -.
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.
FT CHAIN 1..513
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000021573"
FT MOD_RES 145
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 144..146
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 513 AA; 55526 MW; 62195D01547B97BC CRC64;
MTRVINLDGE SLTLEDVIAI ARQGVACRID DSAIEAVNAS RKIVDDIVSE KRVVYGVTTG
FGSLCNVSIS PEDTVQLQEN LIRTHASGFG DPLPEDAVRA IMLIRINSLV KGYSGIRLST
IEKLLELLNK GVHPYIPEKG SLGASGDLAP LAHMVLPMLG LGKAYYKGEF LSGQEALDKA
GIDKISLAAK EGLALINGTT VLTAIGALAT YDAIQLLKLS DLAGALSLEV HNGITSPFEE
NLHTIRPQSG QLATARNIRN LLEGSQNTTV ATQSRVQDPY TLRCMPQIHG ASKDSIAYVK
SKVDIEINSV TDNPIICKDG HVISGGNFHG EPMAQPFDFL GIAISEIGNV SERRVERLVN
SQLSKLPSFL VKYPGLNSGF MITQYACASL ASENKVLAHP ASVDSIPSCE NQEDFVSMGT
TAARKAFEIL KNSRRIVATE IMAACQALDL KPENHELGKG TKVAYDLFRK EVNFIEHDKH
IEIYDELNKA STVIEDPSFL EAVEQAVELS IQF