HUTH_BRUA4
ID HUTH_BRUA4 Reviewed; 511 AA.
AC A6WYU8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=Oant_1435;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS14152.1; -; Genomic_DNA.
DR RefSeq; WP_012091500.1; NC_009667.1.
DR AlphaFoldDB; A6WYU8; -.
DR SMR; A6WYU8; -.
DR STRING; 439375.Oant_1435; -.
DR EnsemblBacteria; ABS14152; ABS14152; Oant_1435.
DR KEGG; oan:Oant_1435; -.
DR PATRIC; fig|439375.7.peg.1504; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_5; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 715502at2; -.
DR PhylomeDB; A6WYU8; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000002301; 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_1000021562"
FT MOD_RES 143
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 142..144
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 511 AA; 53335 MW; 2ECEF4DA296C5679 CRC64;
MTLVLKPGSV PLETLETIYR EGLPVRIDPA FHAGVEKAAA RIAEIAAGDE PVYGINTGFG
KLASIRIAAG DVATLQRNLI LSHCCGVGEP LSENIVRLIM ALKLISLGRG ASGVRLEVIT
LIEDMLKKGV IPMIPEKGSV GASGDLAPLA HMTAAMIGEG EAFYKGERLP SAKALEKAGL
KPVVLAAKEG LALINGTQTS TALALAGLFR AHRAAQTALI TGALSTDAAM GSDAPFHEEI
HTLRGHKGQI DAGRALRALL EGSVIRQSHL EGDQRVQDPY CIRCQPQVDG ACLDILRQAA
RTLEIEANAV TDNPLILSDG RAVSGGNFHA EPVAFAADQI ALAVCEIGAI SQRRIALLVD
PALSFGLPAF LARKPGLNSG LMIAEVTSAA LMSENKQMAH PASVDSTPTS ANQEDHVSMA
CHGARRLLQM TANLNAIIGI EALTGALGVE LREPLTTSPE LAKVIAVLRG KVPTLEDDRY
MADDLKNAAE LVVDGALAGA VSSGILPSLE A