ID A0A091RAF3_MERNU Unreviewed; 662 AA.
AC A0A091RAF3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Histidine ammonia-lyase {ECO:0000256|ARBA:ARBA00017271, ECO:0000256|RuleBase:RU004479};
DE EC=4.3.1.3 {ECO:0000256|ARBA:ARBA00012994, ECO:0000256|RuleBase:RU004479};
GN ORFNames=N331_06576 {ECO:0000313|EMBL:KFQ36486.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ36486.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ36486.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ36486.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-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,
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 -!- SIMILARITY: Belongs to the PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; KK716032; KFQ36486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RAF3; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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; IPR021922; Par3/HAL_N.
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 Pfam; PF12053; Par3_HAL_N_term; 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:UP000052967}.
FT DOMAIN 13..80
FT /note="Par3/HAL N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12053"
SQ SEQUENCE 662 AA; 73034 MW; 690930D774251A2E CRC64;
MPRYTVHVRG EWLAVPCLNG TNTIRWLGKE AVRRYMKNKP DNGGFASVEE VKFYIRRCKG
LGLLDLDDTV EDALEDNEFV EVVIEGDIMS PDFIPSQPEG VHLYSKYREP EQYISLDGNS
LTTEDLVSLG KGLYKIKLTP EAEVKVKKSR EVIERIVKEQ TVVYGITTGF GKFARTVIPN
SKLRELQVNL VRSHSAGVGK PLSPERSRML LALRINVLAK GYSGISLETL QQVIEAFNAS
CLPYIPEKGT VGASGDLAPL SHLALGLIGE GKMWSPKSGW ADAKYVLEAH GLRPITLKPK
EGLALINGTQ MITSLGCEAV ERAGAIARQA DIIAALTLEV LKGTTRAFDT DIHAVRPHRG
QAEVAFRFRS LLDSDHHPSE IAESHRFCDR VQDAYTMRCC PQVHGVVNDT IAFVKDIMTT
EINSATDNPM VFAERAETIS GGNFHGEYPA KALDYLAIGV HELAAISERR IERLCNPSLS
ELPAFLVTEG GLNSGFMIAH CTAAALVSEN KALCHPSSVD SLSTSAATED HVSMGGWAAR
KALRVIEHVE QVLAIELLAA CQGIEFLRPL RTTTPLEKVY DLVRSVVRPW MKDRFMAPDI
EAAHRLLVEQ KASVWEVAKP YIEKYRREHI PESRPISPTA FSLGSLEVNT GVGHDHGHHN
EL
//