ID A0A0P0CY26_9BACT Unreviewed; 501 AA.
AC A0A0P0CY26;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=DC20_16740 {ECO:0000313|EMBL:ALJ00316.1};
OS Rufibacter tibetensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=512763 {ECO:0000313|EMBL:ALJ00316.1, ECO:0000313|Proteomes:UP000061382};
RN [1] {ECO:0000313|EMBL:ALJ00316.1, ECO:0000313|Proteomes:UP000061382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1351 {ECO:0000313|EMBL:ALJ00316.1,
RC ECO:0000313|Proteomes:UP000061382};
RA Dai J.;
RT "Complete genome sequence of Rufibacter tibetensis strain 1351t, a
RT radiation-resistant bacterium from tibet plateau.";
RL Submitted (AUG-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; CP012643; ALJ00316.1; -; Genomic_DNA.
DR RefSeq; WP_062544879.1; NZ_CP012643.1.
DR AlphaFoldDB; A0A0P0CY26; -.
DR STRING; 512763.DC20_16740; -.
DR KEGG; rti:DC20_16740; -.
DR PATRIC; fig|512763.3.peg.3684; -.
DR OrthoDB; 9806955at2; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000061382; 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:UP000061382}.
SQ SEQUENCE 501 AA; 54886 MW; 1D8568BDDE7395B4 CRC64;
MAGQHLVSLA PLSLPEIKKV LQTKATLSLS EEVEQRILRS HAYLHQHLQL APGPVYGINT
GFGALCNTTI SPENLETLQR NLVMSHACGT GEEVPAEVVK LMLFLKVQSL SYGYSGVQLS
TVQRLLSFFN RDVYPIVYQQ GSLGASGDLA PLAHLCLPMI GLGEVRFQEF KLKGNEILDI
FSWEPIRLQA KEGLALLNGT QMMAAYGTLI CLKARQISAA ADVLAALSLE AFDGLSAPFS
PEIHQIRPHP GQLKTAARIL HLLSESELQQ KPKSQVQDPY SFRCVPQVHG ASLDALEYAE
KVFTTEINSV TDNPNVFAEE ELVLSGGNFH GQPLALALDF LSIGLAEWGS ISERRTFQLI
SGQRGLPQFL IQEPGLNSGF MIPQYTAASI VSQNKQLCTP ASVDSIVSSN GQEDHVSMGA
NGATKAYQVV QNVERILAIE LMAAVQALEF RRPLRTSPVL EKVVAAYRTQ VSPLEQDRVL
QPDIEKSVKF IQEFPFEDLM A
//
