ID A0A099T832_9RHOB Unreviewed; 512 AA.
AC A0A099T832;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=PM04_15130 {ECO:0000313|EMBL:KGL00387.1};
OS Thalassobacter sp. 16PALIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobacter.
OX NCBI_TaxID=1225651 {ECO:0000313|EMBL:KGL00387.1, ECO:0000313|Proteomes:UP000029829};
RN [1] {ECO:0000313|EMBL:KGL00387.1, ECO:0000313|Proteomes:UP000029829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16PALIMAR09 {ECO:0000313|EMBL:KGL00387.1,
RC ECO:0000313|Proteomes:UP000029829};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Thalassobacter sp. 16PALIMAR09.";
RL Submitted (MAR-2014) 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}.
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:KGL00387.1}.
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DR EMBL; JHAK01000008; KGL00387.1; -; Genomic_DNA.
DR RefSeq; WP_038008259.1; NZ_JHAK01000008.1.
DR AlphaFoldDB; A0A099T832; -.
DR GeneID; 78125927; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000029829; 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:UP000029829}.
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 512 AA; 53245 MW; 277FF4CB88EA3D73 CRC64;
MTVLTLTPGA VTLADLEKIF REEASVRLDP ACRPAIELAH ARIAKAVAGT DAVYGVNTGF
GKLASVKIEA KDTAALQRNL ILSHCCGVGP AIPRGHARLL MALKLLSLGR GASGVRLEIV
DLIEAMLDKG VTPVIPAQGS VGASGDLAPL AHMAAAMMGH GEAEFGGKVM SGDKALAAAG
LTPVELGPKE GLALINGTQF STAFALAGLF GAWRGAHSAL VTSALSTDAI MGSTAPLQPE
IHALRGHRGQ IEAGETMRAL LAGSEIRDSH VVDDARVQDP YCIRCQPQVT GAAMDVLRMA
ARTLEVEANA ATDNPLVLVG ADLIVSGGNF HAEPVGFAAD MIALAIAEIG AIAQRRVALI
VDPVLSFNLP PFLTPNPGLN SGYMIAEVTT AALMSENKHL ANPCVTDSTP TSANQEDHVS
MAAHGARRLG PMIDNLNCIL GVELLCGAQG IDFRAPLTTS DTLQRVVTRV RQDVATLGED
RYLAPDLERA TRMIASGEIV TAAAIDMPEF DA
//
