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Database: UniProt
Entry: A0A0Q7SWU9_9BURK
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ID   A0A0Q7SWU9_9BURK        Unreviewed;       501 AA.
AC   A0A0Q7SWU9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=ASD35_15590 {ECO:0000313|EMBL:KQY88944.1};
OS   Pelomonas sp. Root1444.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY88944.1, ECO:0000313|Proteomes:UP000051648};
RN   [1] {ECO:0000313|Proteomes:UP000051648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY88944.1, ECO:0000313|Proteomes:UP000051648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1444 {ECO:0000313|EMBL:KQY88944.1,
RC   ECO:0000313|Proteomes:UP000051648};
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:KQY88944.1}.
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DR   EMBL; LMFP01000003; KQY88944.1; -; Genomic_DNA.
DR   RefSeq; WP_056874150.1; NZ_LMFP01000003.1.
DR   AlphaFoldDB; A0A0Q7SWU9; -.
DR   STRING; 1736464.ASD35_15590; -.
DR   OrthoDB; 9806955at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000051648; 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:UP000051648}.
SQ   SEQUENCE   501 AA;  52004 MW;  5F47A3A04EDCE30A CRC64;
     MKLIPGQLTL AQLADIAASR AALQLDDWAP VDQSAALVAA AAAGDAPVYG VNTGFGKLAS
     TRIAKDQLAQ LQLNLIRSHS VGVGAPMSPE VVRLMLATKA GSLARGFSGV RRAVITALLD
     AFNAGFIPYV PAQGSVGASG DLAPLAHLTL ALMGEGEALV AGQRVPARDE LARLGLQPLT
     LAAKEGLALI NGTQASTALA LHALLRFEGL FATALASGAM TLDAARGSDG PFDARIHAVR
     GQPGQMEVAG VYRELLAGSA IRASHREGDE RVQDPYCLRC QPQVMGACLD QARHAAQVLV
     REANAVTDNP LVFDDVMISG GNFHAEPVAF AADNLALAIA EVGAIAERRI AMLIDPGISR
     LPPFLTADAG LHSGFMIAHV TAAALASENK SLAHPASVDS LPTSANQEDH VSMATFAGRR
     LHAMLDNTAH IIAIEMLAAA QGIDFLRPLQ SSAPVEALHT RLRADCASSP ADHYLAPDIE
     RAAALVQAGV LQPPHAPRFN G
//
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