ID A0A077M7Y2_9MICO Unreviewed; 521 AA.
AC A0A077M7Y2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 Name=hutH {ECO:0000313|EMBL:CCI52699.1};
GN ORFNames=BN13_20021 {ECO:0000313|EMBL:CCI52699.1};
OS Tetrasphaera jenkinsii Ben 74.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI52699.1, ECO:0000313|Proteomes:UP000035720};
RN [1] {ECO:0000313|EMBL:CCI52699.1, ECO:0000313|Proteomes:UP000035720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ben 74 {ECO:0000313|EMBL:CCI52699.1,
RC ECO:0000313|Proteomes:UP000035720};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCI52699.1}.
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DR EMBL; CAJC01000112; CCI52699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077M7Y2; -.
DR STRING; 1193518.BN13_20021; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000035720; 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:CCI52699.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035720}.
SQ SEQUENCE 521 AA; 54672 MW; 130392D2AB78B37D CRC64;
MTLGNEPLTI EQVVHIARSA PPGTDYLGRP VSVEVSEAAW GRVRHTRGVI DALADDTVAH
YGISTGFGAL ANTSIPPEKR TQLQRSLIRS HAAGSGAEVE REVVRALMLL RIQTLATGRT
GIREETLRAY VAMLNAGITP VVREYGSLGC SGDLAPLSHC ALALMGEGWV RDADGELMAA
GDALAAADIA PVELREKEGL ALINGTDGML GMLCMAITDL RALVTIADLA AAMSVEGLLG
TDDVFAADLH ALRPQPGQAL SAANMRKVLA VSGIRDSHRD PEACTRVQDA YSLRCAPQVA
GAVRDTLDHA ARVAGWELAS AVDNPVVTLD DRVESNGNFH GAPVAYVLDF LAIAAADLAS
MSERRTDRFL DKARNHGLNA FLADDPGVDS GLMIAQYTAA GMVSEMKRLA VPASVDSIPS
SAMQEDHVSM GWGAARKLRR SVDALTQVLT IELLTAARGI QLRAPLTPSP VSAAIIAALD
EVSRTAPGPD RFLADDIAAA VYAVADGSVR HAAESVAGPL N
//