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Database: UniProt
Entry: A0A0Q6Q7D2_9MICO
LinkDB: A0A0Q6Q7D2_9MICO
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ID   A0A0Q6Q7D2_9MICO        Unreviewed;       527 AA.
AC   A0A0Q6Q7D2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
DE            EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
GN   ORFNames=ASC63_06325 {ECO:0000313|EMBL:KQV08390.1};
OS   Leifsonia sp. Root112D2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV08390.1, ECO:0000313|Proteomes:UP000051914};
RN   [1] {ECO:0000313|EMBL:KQV08390.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08390.1,
RC   ECO:0000313|Proteomes:UP000051914};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV08390.1, ECO:0000313|Proteomes:UP000051914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root112D2 {ECO:0000313|EMBL:KQV08390.1,
RC   ECO:0000313|Proteomes:UP000051914};
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,
CC         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|RuleBase:RU004479}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004480}.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {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:KQV08390.1}.
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DR   EMBL; LMCU01000001; KQV08390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q6Q7D2; -.
DR   STRING; 1736426.ASC63_06325; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000051914; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-EC.
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   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   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808,
KW   ECO:0000256|RuleBase:RU004479};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003954};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051914}.
SQ   SEQUENCE   527 AA;  54159 MW;  5DBE062C6A627BEF CRC64;
     MEQPATASDT ANTATPASVT VGTGAVSFDD VVAVARRGAR IELDPAALDG VRATRAIIDS
     LTDDTEPHYG ISTGFGALAT TYIASDRRAQ LQASLVRSHA AGSGPEVERE VVRALMLLRL
     STLMTGRTGV RAETAETYAA VLNAGITPIV REYGSLGCSG DLAPLAHCAL AVMGEGTVRD
     TNGDERDASD ALAAAGIRPV QLAEKEGLAL INGTDGMLGM LLLALDDLRR LMKTADVAAA
     MSVEALLGTD AVFAADLQAL RPQTGQGLSA ANLRALLAGS PIVASHAGPE DPSVQDAYSL
     RCAPQVHGAA RDTASHAADV AARELESAVD NPVVTLDGRV ESNGNFHGAP IGYVLDFLAI
     AAADVASMSE RRTDRHLDVS RSKGLPPFLA HEAGVDSGLM IAQYTAAGIV SELKRLAVPA
     SVDSIPSSAM QEDHVSMGWA AARKLRRSLD GLGRVLAIEI MTSSRALDLR APLEPGAATG
     AVRALVRSVA SGPGHDRFLS PEIEGVVGLV QSGAVLAAAE GVTGALE
//
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