HUTH_PSEPU
ID HUTH_PSEPU Reviewed; 510 AA.
AC P21310;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=hutH;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90;
RX PubMed=2332400; DOI=10.1128/jb.172.5.2224-2229.1990;
RA Consevage M.W., Phillips A.T.;
RT "Sequence analysis of the hutH gene encoding histidine ammonia-lyase in
RT Pseudomonas putida.";
RL J. Bacteriol. 172:2224-2229(1990).
RN [2]
RP CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=8239649; DOI=10.1006/abbi.1993.1570;
RA Hernandez D., Stroh J.G., Phillips A.T.;
RT "Identification of Ser143 as the site of modification in the active site of
RT histidine ammonia-lyase.";
RL Arch. Biochem. Biophys. 307:126-132(1993).
RN [3]
RP CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, AND MUTAGENESIS OF
RP SER-144.
RX PubMed=8024588; DOI=10.1006/bbrc.1994.1863;
RA Hernandez D., Phillips A.T.;
RT "Ser-143 is an essential active site residue in histidine ammonia-lyase of
RT Pseudomonas putida.";
RL Biochem. Biophys. Res. Commun. 201:1433-1438(1994).
RN [4]
RP CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDRATION AT SER-144, AND
RP MUTAGENESIS OF SER-144.
RX PubMed=8204579; DOI=10.1021/bi00187a011;
RA Langer M., Reck G., Reed J., Retey J.;
RT "Identification of serine-143 as the most likely precursor of
RT dehydroalanine in the active site of histidine ammonia-lyase. A study of
RT the overexpressed enzyme by site-directed mutagenesis.";
RL Biochemistry 33:6462-6467(1994).
RN [5]
RP CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDRATION AT SER-144, AND
RP MUTAGENESIS OF SER-144.
RX PubMed=7947813; DOI=10.1021/bi00251a011;
RA Langer M., Lieber A., Retey J.;
RT "Histidine ammonia-lyase mutant S143C is posttranslationally converted into
RT fully active wild-type enzyme. Evidence for serine 143 to be the precursor
RT of active site dehydroalanine.";
RL Biochemistry 33:14034-14038(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 152 AND
RP 439.
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90;
RX PubMed=10220322; DOI=10.1021/bi982929q;
RA Schwede T.F., Retey J., Schulz G.E.;
RT "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide
RT modification as the catalytic electrophile.";
RL Biochemistry 38:5355-5361(1999).
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:0000269|PubMed:7947813, ECO:0000269|PubMed:8024588,
CC ECO:0000269|PubMed:8204579, ECO:0000269|PubMed:8239649};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By histidine and urocanate.
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.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M35140; AAA25840.1; -; Genomic_DNA.
DR PIR; A35251; A35251.
DR RefSeq; WP_016502005.1; NZ_WOWR01000002.1.
DR PDB; 1B8F; X-ray; 2.10 A; A=2-510.
DR PDB; 1EB4; X-ray; 2.00 A; A=2-510.
DR PDB; 1GK2; X-ray; 1.90 A; A/B/C/D=2-510.
DR PDB; 1GK3; X-ray; 2.25 A; A=2-510.
DR PDB; 1GKJ; X-ray; 1.70 A; A=2-510.
DR PDB; 1GKM; X-ray; 1.00 A; A=2-510.
DR PDBsum; 1B8F; -.
DR PDBsum; 1EB4; -.
DR PDBsum; 1GK2; -.
DR PDBsum; 1GK3; -.
DR PDBsum; 1GKJ; -.
DR PDBsum; 1GKM; -.
DR AlphaFoldDB; P21310; -.
DR SMR; P21310; -.
DR STRING; 1240350.AMZE01000005_gene2503; -.
DR GeneID; 45526576; -.
DR KEGG; ag:AAA25840; -.
DR eggNOG; COG2986; Bacteria.
DR BioCyc; MetaCyc:MON-11608; -.
DR BRENDA; 4.3.1.3; 5092.
DR UniPathway; UPA00379; UER00549.
DR EvolutionaryTrace; P21310; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Histidine metabolism;
KW Lyase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2332400"
FT CHAIN 2..510
FT /note="Histidine ammonia-lyase"
FT /id="PRO_0000161017"
FT MOD_RES 144
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:7947813,
FT ECO:0000269|PubMed:8204579"
FT CROSSLNK 143..145
FT /note="5-imidazolinone (Ala-Gly)"
FT MUTAGEN 113
FT /note="S->A: No loss of activity."
FT MUTAGEN 144
FT /note="S->A,T: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:7947813,
FT ECO:0000269|PubMed:8024588, ECO:0000269|PubMed:8204579"
FT MUTAGEN 144
FT /note="S->C: No effect."
FT /evidence="ECO:0000269|PubMed:7947813,
FT ECO:0000269|PubMed:8024588, ECO:0000269|PubMed:8204579"
FT MUTAGEN 394
FT /note="S->A: No loss of activity."
FT MUTAGEN 419
FT /note="S->A: No loss of activity."
FT CONFLICT 152
FT /note="H -> T (in Ref. 1; AAA25840)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> P (in Ref. 1; AAA25840)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 13..21
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 94..108
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:1GK3"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1GK2"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 199..229
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 248..261
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 286..308
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 333..361
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 383..399
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 421..451
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 478..480
FT /evidence="ECO:0007829|PDB:1GK3"
FT HELIX 483..494
FT /evidence="ECO:0007829|PDB:1GKM"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:1GKM"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:1GKM"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:1GK3"
SQ SEQUENCE 510 AA; 53761 MW; 7D80C7E64B0C4F57 CRC64;
MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED RTAYGINTGF
GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI MVLKINSLSR GFSGIRRKVI
DALIALVNAE VYPHIPLKGS VGASGDLAPL AHMSLVLLGE GKARYKGQWL SATEALAVAG
LEPLTLAAKE GLALLNGTQA STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR
IHEARGQRGQ IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA
AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG SLSERRISLM
MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS HPHSVDSLPT SANQEDHVSM
APAAGKRLWE MAENTRGVLA IEWLGACQGL DLRKGLKTSA KLEKARQALR SEVAHYDRDR
FFAPDIEKAV ELLAKGSLTG LLPAGVLPSL
