ID K0K3L7_SACES Unreviewed; 505 AA.
AC K0K3L7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 OrderedLocusNames=BN6_56620 {ECO:0000313|EMBL:CCH32921.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH32921.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH32921.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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}.
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DR EMBL; HE804045; CCH32921.1; -; Genomic_DNA.
DR RefSeq; WP_015103033.1; NC_019673.1.
DR AlphaFoldDB; K0K3L7; -.
DR STRING; 1179773.BN6_56620; -.
DR KEGG; sesp:BN6_56620; -.
DR PATRIC; fig|1179773.3.peg.5702; -.
DR eggNOG; COG2986; Bacteria.
DR HOGENOM; CLU_014801_4_0_11; -.
DR OrthoDB; 9806955at2; -.
DR BioCyc; SESP1179773:BN6_RS27285-MONOMER; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000006281; Chromosome.
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:UP000006281}.
SQ SEQUENCE 505 AA; 54225 MW; 6D43F0C177E21550 CRC64;
MNGHTITRED YSIDALVEIV RERPELRLAD DVVADIAAGR KFVDELSRRG EHVYGVNTGF
GSLCETRIDS AEVEELQRNH VLSHACGVGE PVPEAVSRLV LLIKLLTLRS GRTGISPGTV
EALIALWNAG VIPAIPARGT VGASGDLAPL AHLSLPLLGL GQVHWEGRLT PAAEALADAG
LAPIRLQAKD GLALTNGVQY INALAAEAVH RATLLTRCAD VVAAVSTQAF SCSDNFYHPL
YHSTSRNRHR HDVVRNLGLL LAGGNHAALP TCNRSRQDPY SFRCLPQVHA AARQVVDFAA
TVVTEECNGV SDNPLFFAEE NLVLMGGNLH GQSTATTLDC LAISLADLSA ISERRSYQLL
SGQRGLPDFL TRNAGLHSGF MVAQYSAAAL VNENKTLASP ASVDTIPTCQ LQEDHVSMGG
TAALKLRQVL DNVEHVLAIE LMLAVQATEL NADLRVSPAT ARVVQDFREV VPALREDRVL
SDDMANARRF LLDNGPLWTE DLGLS
//
