HUTH_PSEA6
ID HUTH_PSEA6 Reviewed; 509 AA.
AC Q15X40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 110.
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=Patl_1022;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000388; ABG39548.1; -; Genomic_DNA.
DR RefSeq; WP_011573889.1; NC_008228.1.
DR AlphaFoldDB; Q15X40; -.
DR SMR; Q15X40; -.
DR STRING; 342610.Patl_1022; -.
DR EnsemblBacteria; ABG39548; ABG39548; Patl_1022.
DR KEGG; pat:Patl_1022; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_6; -.
DR OMA; CAPQVAG; -.
DR OrthoDB; 715502at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000001981; 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 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 3: Inferred from homology;
KW Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..509
FT /note="Histidine ammonia-lyase"
FT /id="PRO_1000021564"
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 509 AA; 54897 MW; C26D26FF3018B2C8 CRC64;
MEQKYLLQPG KLTIETMRQV HRRHVPITLA PDSFERIHSA EQTVRDVITQ GRTVYGINTG
FGLLANTKIE VDELELLQRS IVLSHAAGIG TLMSASTVRL LMLLKINSLA RGYSGIRLIV
IEALIALYNH QVYPAIPEKG SVGASGDLAP LAHMSAVLLG EGEVIYQGNQ ISAEKGLMIA
GLQPISLAPK EGLALLNGTQ ASTAFALQGL FYAENALTSS IAIGALSVDA ALGSRVPFNE
RIHIVRGHQA QIDVATGFRT LLQESEIGKS HGGCEKVQDP YSLRCQPQVM GACLQQMRFA
KQILVTEANG VSDNPIVFSE SDDVLSGGNF HAETVAMAAD MLAIALAEIG ALSERRMALL
IDSSLSGLPP FLVDNGGVNS GFMIAQVTSA ALASENKSYA HPASIDSLPT SANQEDHVSM
ATFAGRRLRD IFDNVAGILA IEWLAASQGI DFRFPLKTST QLQSVHALMR SKVTFYDKDR
YFSPDIEQAK LLITRHSLSD LVQQDIQLL