ID A0A099F7X5_9RHOB Unreviewed; 513 AA.
AC A0A099F7X5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
DE Short=Histidase {ECO:0000256|HAMAP-Rule:MF_00229};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|HAMAP-Rule:MF_00229};
GN Name=hutH {ECO:0000256|HAMAP-Rule:MF_00229};
GN ORFNames=IT41_01140 {ECO:0000313|EMBL:KGJ06810.1}, SAMN04487972_102131
GN {ECO:0000313|EMBL:SFA41415.1};
OS Paracoccus halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ06810.1, ECO:0000313|Proteomes:UP000029846};
RN [1] {ECO:0000313|EMBL:KGJ06810.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ06810.1,
RC ECO:0000313|Proteomes:UP000029846};
RA McGinnis J.M., Wolfgang W.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGJ06810.1, ECO:0000313|Proteomes:UP000029846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ06810.1,
RC ECO:0000313|Proteomes:UP000029846};
RA Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT York State patients.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFA41415.1, ECO:0000313|Proteomes:UP000182312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA41415.1,
RC ECO:0000313|Proteomes:UP000182312};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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, ECO:0000256|HAMAP-
CC Rule:MF_00229, 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|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004479}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229,
CC ECO:0000256|RuleBase:RU004480}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000256|HAMAP-Rule:MF_00229}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000256|HAMAP-
CC Rule:MF_00229, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; JRKN01000001; KGJ06810.1; -; Genomic_DNA.
DR EMBL; FOJO01000002; SFA41415.1; -; Genomic_DNA.
DR RefSeq; WP_036738014.1; NZ_JRKN01000001.1.
DR AlphaFoldDB; A0A099F7X5; -.
DR STRING; 376733.SAMN04487972_102131; -.
DR eggNOG; COG2986; Bacteria.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000029846; Unassembled WGS sequence.
DR Proteomes; UP000182312; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00229; His_ammonia_lyase; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00229};
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00229};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00229};
KW Reference proteome {ECO:0000313|Proteomes:UP000029846}.
FT MOD_RES 144
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
FT CROSSLNK 143..145
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00229"
SQ SEQUENCE 513 AA; 53587 MW; A990D60415CF48A9 CRC64;
MTELILTPGE TTLAQLEQVW RQQSAVRLDD SARAGIAASA ARIAAAANGD VPVYGVNTGF
GKLASIKIAA GDTATLQRNL ILSHCCGVGE SVEPETVRLI MVLKLLSLGR GASGIRPEVV
ALMEDMLARD VLPVIPSQGS VGASGDLAPL AHMAAAMLGE GRATHQGREM PSADALSAAG
LTPVVLAAKE GLALINGTQV STAFALAGLF EGFAAARAAL VVSALSTDAI MGSTAPFLDE
IHTLRGHRGQ ILAARTIRAL MEGSVIRESH REGDTRVQDP YCIRCQPQVT GACLDLLWQA
GRTLEIEANA ATDNPLVLTR ADQIVSGGNF HAEPVAFAAD QIALALAEIG AISQRRIALM
VDPTLSHDLP PFLTPDPGLN SGLMIAEVTS AALMSENKHL ATPCSTDSTP TSANQEDHVS
MAAHGARRLR RMNANLSQII GIEALCAAAG VEFRAPLATS EPLQAVIGRL RATVPALDQD
RYLAPDLAEA ARLIRQGELV AAVPAELLHE VRP
//
