HUTH_RHIME
ID HUTH_RHIME Reviewed; 511 AA.
AC O31197;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=hutH; OrderedLocusNames=RB0831; ORFNames=SMb21165;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RA Uhde C., Schmidt R., Droege M., Jording D., Puehler A., Selbitschka W.;
RT "A Sinorhizobium meliloti hutH-mutant, defective in the histidine degrading
RT enzyme histidase, is impaired in stationary phase survival.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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 -!- INDUCTION: By histidine.
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; AF032903; AAB86963.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49231.1; -; Genomic_DNA.
DR PIR; G95945; G95945.
DR RefSeq; NP_437371.1; NC_003078.1.
DR RefSeq; WP_010975687.1; NC_003078.1.
DR AlphaFoldDB; O31197; -.
DR SMR; O31197; -.
DR STRING; 266834.SM_b21165; -.
DR EnsemblBacteria; CAC49231; CAC49231; SM_b21165.
DR GeneID; 61600807; -.
DR KEGG; sme:SM_b21165; -.
DR PATRIC; fig|266834.11.peg.5762; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_5; -.
DR OMA; CAPQVAG; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001976; Plasmid pSymB.
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 2: Evidence at transcript level;
KW Cytoplasm; Histidine metabolism; Lyase; Plasmid; Reference proteome.
FT CHAIN 1..511
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161022"
FT MOD_RES 143
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000250"
FT CROSSLNK 142..144
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
FT CONFLICT 241..252
FT /note="HTLRGHKGQIDT -> QHCAAIRARSTR (in Ref. 1; AAB86963)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..366
FT /note="YG -> LR (in Ref. 1; AAB86963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 52846 MW; 0592C84DBBF18374 CRC64;
MTVILRPGSV PLSDLETIYW TGAPARLDAA FDAGIAKAAA RIAEIVAGNA PVYGINTGFG
KLASIKIDSS DVATLQRNLI LSHCCGVGQP LTEDIVRLIM ALKLISLGRG ASGVRLELVR
LIEAMLDKGV IPLIPEKGSV GASGDLAPLA HMAAVMMGHG EAFFAGERMK GDAALKAAGL
SPVTLAAKEG LALINGTQVS TALALAGLFR AHRAGQAALI TGALSTDAAM GSSAPFHPDI
HTLRGHKGQI DTAAALRQLL TGSPIRQSHI EGDERVQDPY CIRCQPQVDG ACLDLLRSVA
ATLTIEANAV TDNPLVLSDN SVVSGGNFHA EPVAFAADQI ALAVCEIGAI SQRRIALLVD
PALSYGLPAF LAKKPGLNSG LMIAEVTSAA LMSENKQLSH PASVDSTPTS ANQEDHVSMA
CHGARRLLQM TENLFSIIGI EALAAVQGIE FRAPLTTSPE LQKAAAAVRG VSSSIEEDRY
MADDLKAAGD LVASGRLAAA VSAGILPKLE N
