ID A0A0S8HMM4_9BACE Unreviewed; 507 AA.
AC A0A0S8HMM4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AMS27_05100 {ECO:0000313|EMBL:KPK86416.1};
OS Bacteroides sp. SM23_62_1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703353 {ECO:0000313|EMBL:KPK86416.1, ECO:0000313|Proteomes:UP000051265};
RN [1] {ECO:0000313|EMBL:KPK86416.1, ECO:0000313|Proteomes:UP000051265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62_1 {ECO:0000313|EMBL:KPK86416.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK86416.1}.
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DR EMBL; LJUQ01000034; KPK86416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8HMM4; -.
DR PATRIC; fig|1703353.3.peg.1732; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000051265; 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 507 AA; 56415 MW; 420003B28010300B CRC64;
MANIHQISPA VIDFGQISNI MDGETRLEIS SESAGLIRKC RAYLDKKLSE EDKPFYGINT
GFGSLHDCSI SNGDLGVLQK NLVMSHACGQ GEEVPREVVR LMLFLKIQSL AYGNSGVQLE
TVRRLVDFFN HGIVPVVYQY GSLGASGDLA PLAHMSLPLI GEGEVWYRNR KRNTMPVLKE
SGLEPLVLQS KEGLALLNGT QFMSAYGVYC CLRVFKLSKL ADIIAAISLD AFDGKLEPFH
PIVQKIRPYK GQIETARRIR VLLEGSELMS RPKKHVQDPY SFRCIPQVHG ASKDSIHYVA
YVFKNEINSV TDNPTIFPDE DLIISAGNFH GQPLALALDN LCIAMSELGS ISERRTYQLV
GGYRGLPPYL VAKPGLNSGF MIPQYTAASL VSYNKQLSTP ASVDSIESCQ GQEDHVSMGA
NAAIKAYQVL LNLERILAIE LFNAAQAIEF RRPARTSEYL ESFLDKYRGK VDFIDDDRIM
YPDMNKSVDF LREVDLELKE GFFAGEY
//
