HUTH_RAT
ID HUTH_RAT Reviewed; 657 AA.
AC P21213; Q5EBB8;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=Hal; Synonyms=Huth;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2120224; DOI=10.1016/s0021-9258(17)44737-5;
RA Taylor R.G., Lambert M.A., Sexsmith E., Sadler S.J., Ray P.N.,
RA Mahuran D.J., McInnes R.R.;
RT "Cloning and expression of rat histidase. Homology to two bacterial
RT histidases and four phenylalanine ammonia-lyases.";
RL J. Biol. Chem. 265:18192-18199(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP CATALYTIC ACTIVITY, ENZYME MECHANISM, AND MUTAGENESIS OF SER-254.
RX PubMed=7961661; DOI=10.1016/s0021-9258(18)47009-3;
RA Taylor R.G., McInnes R.R.;
RT "Site-directed mutagenesis of conserved serines in rat histidase.
RT Identification of serine 254 as an essential active site residue.";
RL J. Biol. Chem. 269:27473-27477(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635 AND SER-648, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 ECO:0000269|PubMed:7961661};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC -!- TISSUE SPECIFICITY: Liver and skin.
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; M58308; AAA63491.1; -; mRNA.
DR EMBL; BC089809; AAH89809.1; -; mRNA.
DR PIR; A36087; A36087.
DR RefSeq; NP_058855.1; NM_017159.1.
DR AlphaFoldDB; P21213; -.
DR SMR; P21213; -.
DR DIP; DIP-37290N; -.
DR IntAct; P21213; 1.
DR STRING; 10116.ENSRNOP00000006971; -.
DR iPTMnet; P21213; -.
DR PhosphoSitePlus; P21213; -.
DR PaxDb; P21213; -.
DR PRIDE; P21213; -.
DR Ensembl; ENSRNOT00000006971; ENSRNOP00000006971; ENSRNOG00000004502.
DR GeneID; 29301; -.
DR KEGG; rno:29301; -.
DR UCSC; RGD:68363; rat.
DR CTD; 3034; -.
DR RGD; 68363; Hal.
DR eggNOG; KOG0222; Eukaryota.
DR GeneTree; ENSGT00390000009047; -.
DR HOGENOM; CLU_014801_4_0_1; -.
DR InParanoid; P21213; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 923557at2759; -.
DR PhylomeDB; P21213; -.
DR TreeFam; TF313824; -.
DR Reactome; R-RNO-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00549.
DR PRO; PR:P21213; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004502; Expressed in liver and 1 other tissue.
DR Genevisible; P21213; RN.
DR GO; GO:0005829; C:cytosol; TAS:RGD.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IDA:RGD.
DR GO; GO:0006548; P:histidine catabolic process; ISO:RGD.
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 GO; GO:0006547; P:histidine metabolic process; TAS:RGD.
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; IPR021922; Par3/HAL_N.
DR InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01225; hutH; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Histidine metabolism; Lyase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..657
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161060"
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:0007744|PubMed:22673903"
FT MOD_RES 637
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35492"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 253..255
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
FT MUTAGEN 223
FT /note="S->A: 2.4% of activity."
FT MUTAGEN 254
FT /note="S->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:7961661"
FT MUTAGEN 508
FT /note="S->A: 75% of activity."
FT MUTAGEN 533
FT /note="S->A: 16% of activity."
SQ SEQUENCE 657 AA; 72284 MW; CBED79FC6CD40FA0 CRC64;
MPRYTVHVRG EWLAVPCQDG KLSVGWLGRE AVRRYMKNKP DNGGFTSVDE VRFLVRRCKG
LGLLDNEDLL EVALEDNEFV EVVIEGDVMS PDFIPSQPEG VFLYSKYREP EKYIALDGDS
LSTEDLVNLG KGHYKIKLTS IAEKKVQQSR EVIDSIIKER TVVYGITTGF GKFARTVIPA
NKLQELQVNL VRSHSSGVGK PLSPERCRML LALRINVLAK GYSGISLETL KQVIEVFNAS
CLSYVPEKGT VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLEAH GLKPIVLKPK
EGLALINGTQ MITSLGCEAV ERASAIARQA DIVAALTLEV LKGTTKAFDT DIHAVRPHRG
QIEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTLRCC PQVHGVVNDT IAFVKDIITT
ELNSATDNPM VFASRGETIS GGNFHGEYPA KALDYLAIGV HELAAISERR IERLCNPSLS
ELPAFLVAEG GLNSGFMIAH CTAAALVSES KALCHPSSVD SLSTSAATED HVSMGGWAAR
KALRVIEHVE QVLAIELLAA CQGIEFLRPL KTTTPLEKVY DLVRSVVRPW IKDRFMAPDI
EAAHRLLLDQ KVWEVAAPYI EKYRMEHIPE SRPLSPTAFS LESLRKNSAT IPESDDL
