ID HUTH_BRADU Reviewed; 519 AA.
AC Q89GV3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
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=bll6242;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC51507.1; -; Genomic_DNA.
DR RefSeq; NP_772882.1; NC_004463.1.
DR RefSeq; WP_011088982.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89GV3; -.
DR SMR; Q89GV3; -.
DR STRING; 224911.AAV28_28765; -.
DR EnsemblBacteria; BAC51507; BAC51507; BAC51507.
DR GeneID; 64026003; -.
DR KEGG; bja:bll6242; -.
DR PATRIC; fig|224911.44.peg.6215; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_5; -.
DR InParanoid; Q89GV3; -.
DR OrthoDB; 9806955at2; -.
DR PhylomeDB; Q89GV3; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR01225; hutH; 1.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF7; HISTIDINE AMMONIA-LYASE; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..519
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000160994"
FT MOD_RES 147
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 146..148
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 519 AA; 53119 MW; 755A8C2A49C6A10B CRC64;
MTEQDAAIVV KPGTVSLDDL ARVLAGQPVV LDPSFWPRVE AAAAIVAKAA QADTPVYGIN
TGFGKLASKR IPPDQTALLQ RNLIVSHCCG VGPATPEPIV RLMMALKIIS LGRGASGVRR
EVIEQLQGML ARRVCPLVPQ QGSVGASGDL APLAHMTAVM IGEGQAIVDG KTVSGGEALA
AAGLAPLTLG PKEGLALING TQFSTAYAIS GVLRGFHLAR AALVTGALSV DAAMASTAPF
RPEIQALRGH AGQIAAAATL TALLDGSDIR LSHLEGDERV QDPYCLRCQP QVAGAALDLI
TQTARALIVE ANAVTDNPLV LVETGEIVSG GNFHAEPVAF AADTIALALS EIGAISERRI
ATLVDPALNF GLPPFLTPDP GVNSGFMIAE VTAAALYAEN KQRAAACSID STPTSANQED
HVSMAAHAAR RLADMADNLA AILGIELLVA AQGITLRAPH ATSAPLVAVI AALREQVPAL
GADRYMAGDL AKAAALVEAD ALPAAAIGVL PSDPFPRLA
//
