HUTH_DICDI
ID HUTH_DICDI Reviewed; 539 AA.
AC Q54JI7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Probable histidine ammonia-lyase;
DE Short=Histidase;
DE EC=4.3.1.3;
GN Name=hal; ORFNames=DDB_G0288025;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
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:0000255|PROSITE-ProRule:PRU10122};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by phagocytic stimuli.
CC {ECO:0000269|PubMed:18559084}.
CC -!- PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which
CC is formed autocatalytically by cyclization and dehydration of residues
CC Ala-Ser-Gly. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAL/histidase family. {ECO:0000305}.
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DR EMBL; AAFI02000107; EAL63438.1; -; Genomic_DNA.
DR RefSeq; XP_636944.1; XM_631852.1.
DR AlphaFoldDB; Q54JI7; -.
DR SMR; Q54JI7; -.
DR STRING; 44689.DDB0231727; -.
DR PaxDb; Q54JI7; -.
DR EnsemblProtists; EAL63438; EAL63438; DDB_G0288025.
DR GeneID; 8626419; -.
DR KEGG; ddi:DDB_G0288025; -.
DR dictyBase; DDB_G0288025; hal.
DR eggNOG; KOG0222; Eukaryota.
DR HOGENOM; CLU_014801_4_0_1; -.
DR InParanoid; Q54JI7; -.
DR OMA; CAPQVAG; -.
DR PhylomeDB; Q54JI7; -.
DR BRENDA; 4.3.1.24; 1939.
DR UniPathway; UPA00379; UER00549.
DR PRO; PR:Q54JI7; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016841; F:ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0004397; F:histidine ammonia-lyase activity; ISS:dictyBase.
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; 1.10.275.10; -; 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 PANTHER; PTHR10362; PTHR10362; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR01225; hutH; 1.
DR PROSITE; PS00488; PAL_HISTIDASE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Histidine metabolism; Lyase; Reference proteome.
FT CHAIN 1..539
FT /note="Probable histidine ammonia-lyase"
FT /id="PRO_0000336622"
FT MOD_RES 148
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10122"
FT CROSSLNK 147..149
FT /note="5-imidazolinone (Ala-Gly)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 539 AA; 58946 MW; DC25703A685BF24B CRC64;
MSTTDKIVYL NGNTLKIEDL INIGYRGYNV SITQEVEELI QKGRNVIDDI LKSEKTVYGI
NTGFGLFSDV IIPPDQVKML QVNLIRSHSS GVGTPLTPER TRMLLALRIN VLTKGYSGIT
LETVKRAIKI LNGNCLPLVP EKGTVGASGD LAPLSHLALG MMGEGKMYDF GDSGNTFTSN
LDVDVLEYRN FKFSPANEIL KRQNLTPIEL NAKEGLALIN GTQLITSLGA EAVYRCKVLA
ETANIITAMT FEALKGLTAA YHPLIHAARP HSGQGRVAAF LRSVLHSDQY PSEITLANKD
TKKVQDSYTL RCVPQVHGIV FDTIDFVQGI INTEMNSATD NPMVFDTDEL CGTISGGNFH
GEYPAKALDY LTIGIHELSN ISERRLERLV NSQLSDGLPS FLVNGGGLNS GFMIAHCTSA
ALVSENKVLV HPSSADTIST SSAKEDHVSM GGWSARKCLN VVENVENVLA IELLAACQGL
DFRRPLKTTE PLEAVYQLVR SKVTFMDKDR FIQPDIEEVY KLIRSGQVLN VVNSILNKK
