HUTH_SALTY
ID HUTH_SALTY Reviewed; 506 AA.
AC Q8ZQQ9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=STM0791;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL19728.1; -; Genomic_DNA.
DR RefSeq; NP_459769.1; NC_003197.2.
DR RefSeq; WP_001095227.1; NC_003197.2.
DR AlphaFoldDB; Q8ZQQ9; -.
DR SMR; Q8ZQQ9; -.
DR STRING; 99287.STM0791; -.
DR PaxDb; Q8ZQQ9; -.
DR EnsemblBacteria; AAL19728; AAL19728; STM0791.
DR GeneID; 1252311; -.
DR KEGG; stm:STM0791; -.
DR PATRIC; fig|99287.12.peg.825; -.
DR HOGENOM; CLU_014801_4_0_6; -.
DR OMA; CAPQVAG; -.
DR PhylomeDB; Q8ZQQ9; -.
DR BioCyc; SENT99287:STM0791-MON; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001014; 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..506
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161026"
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 (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 506 AA; 53841 MW; 09DAE20185BF8870 CRC64;
MNTMTLTPGQ LSLSQLYDIW RHPVQLRLDA SAIDGINASV ACVNDIVAEG RTAYGINTGF
GLLAQTRIAD EDLQNLQRSL VLSHAAGVGD PLDDAMVRLI MVLKINSLAR GFSGIRLSVI
EALIALVNAG VYPLIPAKGS VGASGDLAPL AHLSLTLLGE GKARWQGEWL PAQTALKKAG
LEPVALAAKE GLALLNGTQA STAFALRGLF EAQELFASAV VCGALTTEAV LGSRRPFDAR
IHAARGQQGQ IDVARLFRHL LTDTSAIAES HHHCHKVQDP YSLRCQPQVM GACLTQLRQT
KEVLLAEANA VSDNPLVFAD AGEVISGGNF HAEPVAMAAD NLALAIAEIG ALSERRIALM
MDKHMSQLPP FLVKNGGVNS GFMIAQVTAA ALASENKALA HPHSVDSLPT SANQEDHVSM
APAAGRRLWE MAANTRGIIA VEWLAACQGI DLREGLTSSP LLEQARQTLR EQVAHYTQDR
FFAPDIECAT ALLAQGALQR LVPDFM