HUTH_RHORT
ID HUTH_RHORT Reviewed; 514 AA.
AC Q2RUU3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=Rru_A1301;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=269796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX PubMed=21886856; DOI=10.4056/sigs.1804360;
RA Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA Roberts G.P., Reslewic S., Schwartz D.C.;
RT "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL Stand. Genomic Sci. 4:293-302(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; CP000230; ABC22102.1; -; Genomic_DNA.
DR RefSeq; WP_011389056.1; NC_007643.1.
DR RefSeq; YP_426389.1; NC_007643.1.
DR AlphaFoldDB; Q2RUU3; -.
DR SMR; Q2RUU3; -.
DR STRING; 269796.Rru_A1301; -.
DR EnsemblBacteria; ABC22102; ABC22102; Rru_A1301.
DR KEGG; rru:Rru_A1301; -.
DR PATRIC; fig|269796.9.peg.1367; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_5; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 715502at2; -.
DR PhylomeDB; Q2RUU3; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001929; 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 PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01225; hutH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..514
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000071787"
FT MOD_RES 145
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
FT CROSSLNK 144..146
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00229"
SQ SEQUENCE 514 AA; 52973 MW; 8A8D4F9B9C81A024 CRC64;
MTEPLCLTPG GLSLDVLRRI HREAPPLTLD PRSYAAMAAS QAVVAAIAGG ESAVYGINTG
FGKLAHKRIA PADLEALQTN LILSHATGMG APIADATVRL ILAIKAASLA VGASGIRAEI
VDALLALANA DVLPVIPSKG SVGASGDLAP LAHLCCALLG IGSVRHKGAV LPAGEGLAIA
GLSPITLRAK EGLALINGTQ VSTALALAGL FEIERAFAAA ILAGALSVEA VMGSHRPFDP
RISALRGQFG QIDVAALFRL LLDGSPLNAA HQGPSCERVQ DPYSLRCQPQ VMGAVLDQMR
FAARTLTIEA NGVTDNPLVL VDTGEVLSGG NFHAEPVAMA ADQLAIAASE IGALSERRIA
MLIDSTISGL PPFLVAEPGL NSGFMIAHVT AAALASENKS LAHPASVDSL PTSANQEDHV
SMATFAARRL GDIAANVTGI VGIELLAAAQ GLEFHRPLRS SQTLETAMAM IRERVPSYRV
DRYFAPDLEA IAHLIGEGRF DALVPVDLST LGSV