ID A0A0C5FSQ3_9ACTN Unreviewed; 511 AA.
AC A0A0C5FSQ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=TU94_03500 {ECO:0000313|EMBL:AJP00698.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP00698.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP00698.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP00698.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-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}.
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DR EMBL; CP010849; AJP00698.1; -; Genomic_DNA.
DR RefSeq; WP_044379136.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5FSQ3; -.
DR STRING; 477245.TU94_03500; -.
DR KEGG; scw:TU94_03500; -.
DR PATRIC; fig|477245.3.peg.774; -.
DR HOGENOM; CLU_014801_4_0_11; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000032234; 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:UP000032234}.
SQ SEQUENCE 511 AA; 53085 MW; 13CE1C1B6FD0D93C CRC64;
MTVVVGVGPL SAGEVVSVAR LGTPVALAPE ALKEIARSRE VVQALADDAK PHYGVSTGFG
ALATRHIPTE LRAQLQRSLV RSHAAGSGPE VEREVVRALM LLRLSTLATG RTGVRTQTAE
TYAALLNAGI TPVVHEYGSL GCSGDLAPLA HCALAVMGEG EVRTADGVRK PAAEALAEAG
IAPVVLEEKE GLALINGTDG MLGMLVLAAH DLRRLLRTAD IAAAMSVEGQ LGTDAVFAAD
LQALRPHPGQ ADSAGNLRSL LADSAIVASH KGPECTRVQD AYSLRCTPQV HGTARDTLAH
AELVAYRELA SAVDNPVVTL DGRVESNGNF HGAPVAAVLD FLAISVADVA SISERRTDRF
LDPARNRGLN AFLADDPGVD SGHMIAQYTQ AAIVSELKRL AAPASVDSIP SSAMQEDHVS
MGWSAARKLR RAIDGLGRVL AVELYTAARA LDLRAPLTPG PATAAVRDGL RETVEGPGTD
RWLAPEIEAA VQYVASGRAL AAAESVTGPL A
//
