HUTH_VIBPA
ID HUTH_VIBPA Reviewed; 511 AA.
AC Q87Q77;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=VP1273;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC59536.1; -; Genomic_DNA.
DR RefSeq; NP_797652.1; NC_004603.1.
DR RefSeq; WP_011105800.1; NC_004603.1.
DR AlphaFoldDB; Q87Q77; -.
DR SMR; Q87Q77; -.
DR STRING; 223926.28806261; -.
DR EnsemblBacteria; BAC59536; BAC59536; BAC59536.
DR GeneID; 1188778; -.
DR KEGG; vpa:VP1273; -.
DR PATRIC; fig|223926.6.peg.1213; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_6; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000002493; Chromosome 1.
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..511
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161048"
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 511 AA; 55009 MW; C708D71E41094CDC CRC64;
MLNLTLKPGH ISLNELRQVS RSPVNLTLDP EAIPGIEEST QVVDRVIAED RTVYGINTGF
GLLANTRIAP EDLETLQRSI VLSHAAGIGK FMSDETVRLM MVLKINSLAR GFSGIRLKVI
NMLIDLVNAQ VYPCVPQKGS VGASGDLAPL AHMSTVLLGE GQARHNGQIV SGYEALKIAG
LEPITLAPKE GLALLNGTQA STAFALEGLF IAEDLFASAT VCGAMSVEAA LGSRRPFDPR
IHRVRGHRST MDAAMAYRHL LDTSSEIGES HTNCEKVQDP YSLRCQPQVM GACLQQIRNS
AEVLQVEANS VSDNPLVFAE DNDIISGGNF HAEPVAMAAD NLALAIAEIG SLSERRMALL
IDSALSKLPP FLVDNGGVNS GFMIAQVTSA ALASENKTLA HPASVDSLPT SANQEDHVSM
ATFAARRLKE MGENTRGILA VEYLSAAQGL DFRAPNKSSE RIEIAKQMLR EKVSFYDKDR
YFAPDIEQAN TLLKLALHNA LMPENLLPSV H