HUTH_STRAW
ID HUTH_STRAW Reviewed; 512 AA.
AC Q82I33;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=SAV_3325;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(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 Cys-Ser-Gly. {ECO:0000255|HAMAP-Rule:MF_00229}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000255|HAMAP-
CC Rule:MF_00229}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC71036.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000030; BAC71036.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_037644951.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82I33; -.
DR SMR; Q82I33; -.
DR STRING; 227882.SAV_3325; -.
DR EnsemblBacteria; BAC71036; BAC71036; SAVERM_3325.
DR KEGG; sma:SAVERM_3325; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_11; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 715502at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000000428; 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; Reference proteome.
FT CHAIN 1..512
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161036"
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 (Cys-Gly)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 512 AA; 52953 MW; F2F448B9F3EAF569 CRC64;
MHTVVVGTSG VTASDVLAVA RGGARIELSG EAVTALAAAR GIVDALAAKP EPVYGVSTGF
GALATRHISQ ELRAQLQRNI VRSHAAGMGP RVEREVVRAL MFLRLKTVCS GHTGVRPEVA
QTMADILNAG ITPVVHEYGS LGCSGDLAPL SHCALTLMGE GDAEGPDGTV RPAGDLLAEH
GITPVELREK EGLALLNGTD GMLGMLVMAL ADLDALYKSA DITAALSLEA LLGTDKVLAP
ELHAIRPHPG QGASAANMLA VLAGSELTGH HQDDAPRVQD AYSVRCAPQV AGAGRDTLAH
ARLVAERELA SAVDNPVVLP DGRVESNGNF HGAPVAYVLD FLAIAAADLG SIAERRTDRL
LDKNRSHGLP PFLADDAGVD SGLMIAQYTQ AALVSEMKRL AVPASADSIP SSAMQEDHVS
MGWSAARKLR TAIDNLTRIV AIELYAATRA IELREGLTPA PASQAVITAV RKAGVEGPGP
DRFLAPDLAA ADAFVRDGSL VTAAETVTGP LA