HUTH_YERE8
ID HUTH_YERE8 Reviewed; 507 AA.
AC A1JSW6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=YE4094;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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}.
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; AM286415; CAL14111.1; -; Genomic_DNA.
DR RefSeq; YP_001008235.1; NC_008800.1.
DR AlphaFoldDB; A1JSW6; -.
DR SMR; A1JSW6; -.
DR STRING; 393305.YE4094; -.
DR EnsemblBacteria; CAL14111; CAL14111; YE4094.
DR KEGG; yen:YE4094; -.
DR PATRIC; fig|393305.7.peg.4357; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_6; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000000642; 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.
FT CHAIN 1..507
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000336591"
FT MOD_RES 141
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 140..142
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 507 AA; 54655 MW; 6FA0243713458ECD CRC64;
MTLRPGQMTL ADLRHIYQHP VKITLDESAY APIQQSVDCV QKILAEKRTA YGINTGFGLL
ASTRIATEDL ENLQRSIVLS HAAGVGEPND DAIVRLIMVL KINSLARGFS GIRLEVIQAL
ITLVNAQVYP HIPLKGSVGA SGDLAPLAHM SLLLLGEGKA RYQGEWLDAR AALAKAGLQP
LTLAAKEGLA LLNGTQVSTA YALRGLFEAE DLYAAASVFG SLTVEAALGS RSPFDARIHA
VRGQRGQIDA ARTYRHLLGE RSEVSESHRN CDKVQDPYSL RCQPQVMGAC LTQMRQAAEV
LAIESNAVSD NPLVFADQGD VLSGGNFHAE PVAMAADNLA LALAEIGSLA ERRISLLMDK
HMSQLPPFLV ENGGVNSGFM IAQVTAAALT SENKGLAFPS SVDSIPTSAN QEDHVSMAPR
AGKRLWEMAE NVRGILAVEW LAACQGLDLR KGLKTSDALE PARLLLRKHV AYYEKDRFFA
PDIEAASQLI ALRHMNELMP AHLLPSL