HUTH_STRGC
ID HUTH_STRGC Reviewed; 513 AA.
AC A8AZ70;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=SGO_1811;
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX PubMed=17720781; DOI=10.1128/jb.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(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; CP000725; ABV10192.1; -; Genomic_DNA.
DR RefSeq; WP_012130845.1; NC_009785.1.
DR AlphaFoldDB; A8AZ70; -.
DR SMR; A8AZ70; -.
DR STRING; 467705.SGO_1811; -.
DR EnsemblBacteria; ABV10192; ABV10192; SGO_1811.
DR KEGG; sgo:SGO_1811; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_9; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001131; Chromosome.
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; Reference proteome.
FT CHAIN 1..513
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000078235"
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; 55505 MW; 6FFCC83EEC55B9F6 CRC64;
MTHVINLDGE HLTLEDVIAV ARHGATCEID QEAKKAVEAS RKIVDDIVRE KRVVYGVTTG
FGSLCNVSIS PEDTTQLQEN LIRTHASGFG DPLPEDAVRA IMLIRINSLV KGYSGIRLST
VEKLLELLNK GVVPFIPEKG SLGASGDLAP LAHMVLPMLG LGHAYYQGQL LSGQEALDKA
GIEKIALAAK EGLALINGTT VLTGIGALAT YDAIQLLKLS DVAGALSMEV HNGITSPFEE
DLHTIRPQSG QLATARNIRN LLEGSGNTTV ATQQRVQDPY TLRCIPQIHG ASKDSIAYVK
TKVEIEINSV TDNPIITKEG HVISGGNFHG EPMAQPFDFL GIAISEIGNV SERRVERLVN
SQLSKLPSFL VKHPGLNSGF MITQYACASL ASENKVLAHP ASVDSIPSCE NQEDFVSMGT
TAARKAAEIL KNSRRIVATE IMAACQALDL KPENHELGKG TKPAYDLFRQ HVRFIEFDKD
IEIYEELNKA SELIESDEFL AAVENAVDLS IQF