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 24-JAN-2024, entry version 144. 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; Pseudomonadota; 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 GeneID; 45526576; -. DR KEGG; ag:AAA25840; -. DR eggNOG; COG2986; Bacteria. DR OrthoDB; 9806955at2; -. DR BioCyc; MetaCyc:MONOMER-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; 1.20.200.10; 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 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 //