HUTH_DEIRA
ID HUTH_DEIRA Reviewed; 524 AA.
AC Q9RZ06;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=hutH; OrderedLocusNames=DR_A0147;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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 -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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}.
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DR EMBL; AE001825; AAF12216.1; -; Genomic_DNA.
DR PIR; F75610; F75610.
DR RefSeq; NP_285471.1; NC_001264.1.
DR RefSeq; WP_010889407.1; NZ_CP015082.1.
DR AlphaFoldDB; Q9RZ06; -.
DR SMR; Q9RZ06; -.
DR STRING; 243230.DR_A0147; -.
DR EnsemblBacteria; AAF12216; AAF12216; DR_A0147.
DR KEGG; dra:DR_A0147; -.
DR PATRIC; fig|243230.17.peg.3034; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_0; -.
DR InParanoid; Q9RZ06; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 715502at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000002524; Chromosome II.
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..524
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161002"
FT REGION 500..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 140
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250"
FT CROSSLNK 139..141
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 524 AA; 55536 MW; D7E7E32F139C6661 CRC64;
MILDRDLNLE QFISVVRHGE QVELSAAARE RIARARTVIE QIVEGDTPIY GVNTGFGKFE
NVQIDRSQLA QLQHNLIVSH AIGMGEPLPA EVVRGMLLLR AQSLSLGHSG VRVEVVELLL
ALLNADALPV VPSQGSVGAS GDLAPLAHLA LGLIGLGDIE YQGQVRPAAD VLAELGLSPV
QLQAKEGLAL INGTQLMGSL LALALHDAQV LLGTANLAAA MTVEARYGSH RPFQPDVVGL
RPHPGALAVA AELREFLAGS EIAPSHLTGD GKVQDAYSLR AVPQVHGATW DALAQAERVL
AVEFASVTDN PLIFPETGEV VSGGNFHGQP LAVTIDALKV AVAELGSISE RRTEQLLNPA
LSGLPAFLTP NGGLNSGFMI AQYTSAALVS ENKVLSHPAS VDSIPTSANQ EDHVSMGAHA
ARQLRQIVAN VQTVLSIELL CAAQGLDFQQ LRAGRGVQAA YEYVRTFVPT LTEDRYFRPD
LLRLRGELVS GELLRVAQAA DTQAPAPAKL PDSGDEDRDT TSRH