ID A8XR88_CAEBR Unreviewed; 747 AA.
AC A8XR88;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 87.
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 Name=haly-1 {ECO:0000313|WormBase:CBG17560};
GN Synonyms=Cbr-haly-1 {ECO:0000313|EMBL:CAP35185.2};
GN ORFNames=CBG17560 {ECO:0000313|WormBase:CBG17560}, CBG_17560
GN {ECO:0000313|EMBL:CAP35185.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP35185.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP35185.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP35185.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600959; CAP35185.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XR88; -.
DR STRING; 6238.A8XR88; -.
DR WormBase; CBG17560; CBP45866; WBGene00037154; Cbr-haly-1.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_4_0_1; -.
DR InParanoid; A8XR88; -.
DR OMA; GTRRNFH; -.
DR OrthoDB; 1030318at2759; -.
DR UniPathway; UPA00379; UER00549.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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:UP000008549}.
FT DOMAIN 45..120
FT /note="Par3/HAL N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12053"
SQ SEQUENCE 747 AA; 82803 MW; F9BC673F3A4184E9 CRC64;
MTIDSRKKVQ PEEDDGEDVT IQHCPPIFAS FEIQQSLPTV VCDKMRLQVQ IGTECLVVPC
KPEDTVHSVA RKSVEKLRRL RPKLPLADNY FEVRRTIGNS LLDPEDLVSD VLKDSDFIIV
AANVEETEDA KEAKKQEEID NARAELDRID NRRRKLVFFF LPKLKRNFFR VSFADALAPM
VLAPPTKLII LDGNSLLPED LVRCEKGECA IQLSMEAEVK IKKARTFLEK IASEHRPVYG
ITTGFGTFSN VTIPPEKIKK LQLNLIRSHA TGYGEPLAPN RARMLLALRI NILAKGHSGI
SVENIKKMIA AFNAFCVSYV PQQGTVGCSG DLCPLAHLAL GLLGEGKMWS PNTGWGPADA
VLKKNNLEPL VLGPKEGLAL INGTQMVTAL GAFTLERAHN IARQADVIAA LSLDVLKGTT
RAYDPDIHRI RPHRGQNLSA LRLRALLHSE ANPSQIAESH RNCSKVQDAY TLRCVPQVHG
VVHDTIEFVR EIITTEMNSA TDNPLVFADR EEIISGGNFH GEYPAKALDY LAIAVAELAQ
MSERRLERLV NKELSGLPTF LTPDGGLNSG FMTVQLCAAS LVSENKVLCH PSSVDSIPTS
CNQMINIRIF QEDHVSMGGF SARKALTVVE HVEAVLAMEL LAACQGIEFL KPLMSTAPLH
KVYTLVRSVA PPLNEDRYMK PEIDAVVEMI RENKIWETVL PHLETLEAME ELDPDALRQF
AKTPTGIVQD RSLIPITDSE EEEEDDD
//