ID A0A0R2TU41_9FLAO Unreviewed; 500 AA.
AC A0A0R2TU41;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=ABR90_03730 {ECO:0000313|EMBL:KRO90334.1};
OS Cryomorphaceae bacterium BACL29 MAG-121220-bin8.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655598 {ECO:0000313|EMBL:KRO90334.1, ECO:0000313|Proteomes:UP000051665};
RN [1] {ECO:0000313|EMBL:KRO90334.1, ECO:0000313|Proteomes:UP000051665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL7 MAG-121220-bin8 {ECO:0000313|EMBL:KRO90334.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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}.
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:KRO90334.1}.
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DR EMBL; LICI01000008; KRO90334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TU41; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000051665; 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003954}.
SQ SEQUENCE 500 AA; 55610 MW; 7267C806134011F0 CRC64;
MTFKYGIDKL TVSKIIAIAQ GKMQAELTIQ SIQTIKECRA KVEKMANGLK GFYGINTGFG
PLCDVQITPV ETSILQNNLL LTHAVGVGKN IDKQLSKIMM ICKVHALCQG FSGVRLALIE
RIIYFIEHDL LPTVPEQGSV GASGDLAPLS HLFLPLIGEG EFWINEDIFP AKEVLAKHQL
EIIQLEAKEG LGLINGTQFI LAHTITGLIK MEYLLDLADV SGAMSIEGYK GSSAPFREEL
HEIRPFKGCI KVAERMRNLF KDSQNIASHE NCERVQDPYS MRCIPQVHGA SRNAYSHLLE
LAEIEMNSVT DNPIILSDSE AISGGNFHGQ PLAMALDYCS IAASELGNIA DRRCYLLLEG
KYNLPRLLTK EGGLNSGFMI PQYTTAALVT ENKSLCFPPS ADSIPTGLGQ EDHVSMGSIS
GRQFNQILEN LEKIIAIELM YAAQALEFRR PNTFSKIIEK NHNIIRREVK KLENDRLLKD
DIKKMIQMVE NKKFIVKYDV
//
