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Database: UniProt
Entry: A0A0S9CKZ9_9SPHN
LinkDB: A0A0S9CKZ9_9SPHN
Original site: A0A0S9CKZ9_9SPHN 
ID   A0A0S9CKZ9_9SPHN        Unreviewed;       506 AA.
AC   A0A0S9CKZ9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
DE            Short=Histidase {ECO:0000256|HAMAP-Rule:MF_00229};
DE            EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
GN   Name=hutH {ECO:0000256|HAMAP-Rule:MF_00229};
GN   ORFNames=ASE95_05745 {ECO:0000313|EMBL:KQN94333.1};
OS   Sphingomonas sp. Leaf231.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736301 {ECO:0000313|EMBL:KQN94333.1, ECO:0000313|Proteomes:UP000051427};
RN   [1] {ECO:0000313|EMBL:KQN94333.1, ECO:0000313|Proteomes:UP000051427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf231 {ECO:0000313|EMBL:KQN94333.1,
RC   ECO:0000313|Proteomes:UP000051427};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN94333.1, ECO:0000313|Proteomes:UP000051427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf231 {ECO:0000313|EMBL:KQN94333.1,
RC   ECO:0000313|Proteomes:UP000051427};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:0000256|ARBA:ARBA00000171, ECO:0000256|HAMAP-
CC         Rule:MF_00229, ECO:0000256|RuleBase:RU004479};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00005113, ECO:0000256|HAMAP-Rule:MF_00229,
CC       ECO:0000256|RuleBase:RU004479}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
CC       ECO:0000256|RuleBase:RU004480}.
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:0000256|HAMAP-Rule:MF_00229}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00229, ECO:0000256|RuleBase:RU003954}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQN94333.1}.
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DR   EMBL; LMLS01000001; KQN94333.1; -; Genomic_DNA.
DR   RefSeq; WP_056632562.1; NZ_LMLS01000001.1.
DR   AlphaFoldDB; A0A0S9CKZ9; -.
DR   STRING; 1736301.ASE95_05745; -.
DR   OrthoDB; 9806955at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000051427; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229};
KW   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW   Rule:MF_00229};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00229};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051427}.
FT   MOD_RES         140
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT   CROSSLNK        139..141
FT                   /note="5-imidazolinone (Ala-Gly)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ   SEQUENCE   506 AA;  52168 MW;  E044C2E4B6B57A72 CRC64;
     MILHPGTIAY DQWLAIYRGA APRLDPACAS GIAASVAAVA RIVARGEPVY GINTGFGKLA
     SVRIDASDLA TLQRNIVLSH AAGVGEAMPV PVARLMMALK LASLAQGASG VQPATIALIE
     AMLARGLTPV VPAQGSVGAS GDLAPLAHMT AAMIGVGEMI VDGNAVPSMR ALEDAGLAPL
     VLGPKEGLAL LNGTQFSTAY ALAGLFEAER LYRSALVTGI VSTEAAKGSD APFDPRIHAL
     RGHRGQIDTA DALRAMMAGS AIRASHREND VRVQDPYCLR CQPQVMGAIL DLLRQAAATL
     VTEANGVSDN PLIFPETDEA LSGGNFHAEP VAFAADMIAM ALCEIGSLSE RRIAMLVDPA
     LSGLPAFLTP RPGLNSGFMI PQVTAAALVS ENKQRAFPAS VDSIPTSANQ EDHVSMAAHG
     ARRLIAMAAN VDAVIGIELL AATQGCDFHA PLTSSAPVER VRALLRAQVS TLLDDRHMAP
     DMAVATALVV EGALLTEVGA LPGLAA
//
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