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Database: UniProt
Entry: A0A0A0JQP0_9MICO
LinkDB: A0A0A0JQP0_9MICO
Original site: A0A0A0JQP0_9MICO 
ID   A0A0A0JQP0_9MICO        Unreviewed;       521 AA.
AC   A0A0A0JQP0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=N803_12660 {ECO:0000313|EMBL:KGN37906.1};
OS   Knoellia subterranea KCTC 19937.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN37906.1, ECO:0000313|Proteomes:UP000030011};
RN   [1] {ECO:0000313|EMBL:KGN37906.1, ECO:0000313|Proteomes:UP000030011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN37906.1,
RC   ECO:0000313|Proteomes:UP000030011};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia subterranea.";
RL   Submitted (AUG-2013) 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:KGN37906.1}.
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DR   EMBL; AVPK01000004; KGN37906.1; -; Genomic_DNA.
DR   RefSeq; WP_035904313.1; NZ_AVPK01000004.1.
DR   AlphaFoldDB; A0A0A0JQP0; -.
DR   STRING; 1385521.N803_12660; -.
DR   eggNOG; COG2986; Bacteria.
DR   OrthoDB; 9806955at2; -.
DR   UniPathway; UPA00379; UER00549.
DR   Proteomes; UP000030011; 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|RuleBase:RU003954, ECO:0000313|EMBL:KGN37906.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030011}.
FT   REGION          256..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..288
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  54806 MW;  D1D513F2309791B4 CRC64;
     MTDTAPSQQS ITLGDGPLRI DDIVRVARHG ARVELSPVAL DAVRATRGTI EGLANDTVPH
     YGVSTGFGAL ATRHIPVELR AQLQRSLVRS HAAGAGPEVE REVVRALMLL RIATLATGRT
     GIRPKTLETY LQILNAGITP VVHEYGSLGC SGDLAPLSHC ALALMGEGLV RNDDGEVMDA
     ADALAAAGIT PVELAEKEGL ALINGTDGML GMLCLAITDL RQLVTTADIS AAMSVEGLMG
     SDAPFAADLH ALRPQPGQAR SAENMRKVLS GSPIRDSHRD KESDTRVQDA YSLRCAPQVA
     GGVRDTIDHA ARVAEWELAS AIDNPVVTLD GRVESNGNFH GAPVAYVLDF LAIVAADLAS
     ISERRTDRFL DKARNHELPP FLADDPGVDS GLMIAQYTQA AMVSEMKRLA NPASVDSIPS
     SAMQEDHVSM GWSAARKLRR SVDALTRVVA IELITAARGI QLRAPLEPAP ATAAVIAALA
     ESGNVAPGPD RFLAPDIEAA YEAVVDGTVV TAAETVTGRL N
//
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