ID   HUTH_BOVIN              Reviewed;         657 AA.
AC   A7YWP4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Histidine ammonia-lyase;
DE            Short=Histidase;
DE            EC=4.3.1.3;
GN   Name=HAL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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|PROSITE-ProRule:PRU10122};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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; BC134685; AAI34686.1; -; mRNA.
DR   RefSeq; NP_001098910.1; NM_001105440.1.
DR   AlphaFoldDB; A7YWP4; -.
DR   SMR; A7YWP4; -.
DR   STRING; 9913.ENSBTAP00000021649; -.
DR   PaxDb; A7YWP4; -.
DR   PRIDE; A7YWP4; -.
DR   Ensembl; ENSBTAT00000021649; ENSBTAP00000021649; ENSBTAG00000016276.
DR   GeneID; 615205; -.
DR   KEGG; bta:615205; -.
DR   CTD; 3034; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016276; -.
DR   VGNC; VGNC:29744; HAL.
DR   eggNOG; KOG0222; Eukaryota.
DR   GeneTree; ENSGT00390000009047; -.
DR   HOGENOM; CLU_014801_4_0_1; -.
DR   InParanoid; A7YWP4; -.
DR   OMA; CAPQVAG; -.
DR   OrthoDB; 923557at2759; -.
DR   TreeFam; TF313824; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000016276; Expressed in oocyte and 26 other tissues.
DR   ExpressionAtlas; A7YWP4; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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   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   2: Evidence at transcript level;
KW   Histidine metabolism; Lyase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..657
FT                   /note="Histidine ammonia-lyase"
FT                   /id="PRO_0000336621"
FT   MOD_RES         254
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT   MOD_RES         396
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35492"
FT   MOD_RES         635
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21213"
FT   MOD_RES         637
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35492"
FT   MOD_RES         648
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35492"
FT   CROSSLNK        253..255
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   657 AA;  72291 MW;  9DE5180F223158C5 CRC64;
     MPRYTVHVRG EWLAVPCQDA QLTVGWLGRE AVRRYIKNKP DNGGFASVDD ARFLVRRCKG
     LGLLDNEDPL DVALEDNEFV EVVIEGDAMS PDFIPSQPEG VYLYSKYREP EKYIALDGDS
     LTTEDLVSLG KGHYKIKLTP TAEKRVQKSR EVIDRIVEEK TVVYGITTGF GKFARTVIPV
     SKLEELQFNL VRSHSSGVGK PLSPERCRML LALRINVLAK GYSGISLGTL KQVIEVFNAS
     CLPYVPEKGT VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLAAH GLKPIVLKPK
     EGLALINGTQ MITSLGCEAV ERASAIARQA DIVAALTLEV LKGTTKAFDT DIHAVRPHRG
     QVEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC PQVHGVVNDT IAFVKNIITT
     EINSATDNPM VFASRGETIS GGNFHGEYPA KALDYLAIGV HELASISERR IERLCNPSLS
     ELPAFLVAEG GLNSGFMIAH CTAAALVSEN KALCHPSSVD SLSTSAATED HVSMGGWAAR
     KALRVIEHVE QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI
     EAAHRLLVEQ KVWEVAAPYI EKYRMEHIPE SRPVSPTAFS LEFLHKKSTK IPESEDL