HUTI_DICDI
ID HUTI_DICDI Reviewed; 426 AA.
AC Q55CY3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable imidazolonepropionase;
DE EC=3.5.2.7;
DE AltName: Full=Amidohydrolase domain-containing protein 1 homolog;
GN Name=amdhd1; ORFNames=DDB_G0269854;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate;
CC Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928,
CC ChEBI:CHEBI:77893; EC=3.5.2.7;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC Note=Binds 1 zinc or iron ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC HutI family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72277.1; -; Genomic_DNA.
DR RefSeq; XP_646348.1; XM_641256.1.
DR AlphaFoldDB; Q55CY3; -.
DR SMR; Q55CY3; -.
DR STRING; 44689.DDB0266532; -.
DR MEROPS; M38.980; -.
DR PaxDb; Q55CY3; -.
DR EnsemblProtists; EAL72277; EAL72277; DDB_G0269854.
DR GeneID; 8617303; -.
DR KEGG; ddi:DDB_G0269854; -.
DR dictyBase; DDB_G0269854; amdhd1.
DR eggNOG; KOG3968; Eukaryota.
DR HOGENOM; CLU_041647_2_0_1; -.
DR InParanoid; Q55CY3; -.
DR OMA; CAPHARW; -.
DR PhylomeDB; Q55CY3; -.
DR Reactome; R-DDI-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00551.
DR PRO; PR:Q55CY3; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050480; F:imidazolonepropionase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd01296; Imidazolone-5PH; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR005920; HutI.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR42752; PTHR42752; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01224; hutI; 1.
PE 3: Inferred from homology;
KW Histidine metabolism; Hydrolase; Iron; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..426
FT /note="Probable imidazolonepropionase"
FT /id="PRO_0000328424"
FT BINDING 158
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000250|UniProtKB:P42084"
FT BINDING 158
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
FT BINDING 192
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000250|UniProtKB:P42084"
FT BINDING 260
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:A0KF84"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P42084"
FT BINDING 263
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000250|UniProtKB:P42084"
FT BINDING 334
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000250|UniProtKB:A0KF84"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P42084"
FT BINDING 336
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
SQ SEQUENCE 426 AA; 46887 MW; 0130BE38EAE04726 CRC64;
MGFDFKLKIS NASQLVVISK GKPFLIGKEM SNIEIIENGT MIIDENGIIF DIGTFKEMEE
KYKDKSFEKV LDCTGKSVLP GFVDGHTHPV FSGDRVHEFA MKLAGATYLD VHKAGGGIQF
TISHTKNSTE DELYQLLIPR LNRMLKNGTT LIEAKSGYGL ETETEMKMLK VLDRASKQFQ
GVEIVSTYLG GHAIPKGMNA SEATDDIINK QIPELKRLKD AGEISPANID VFLEKGFFEY
EDTKRILQAG KDIGLECNFH GDELSYMKSG ELAGELGCRA ISHLEKVSED GMKAMAATPT
FAVLLPTTAY ILRLECPPAR RMIELGVPVA LGSDFNPNAH CLSMPFVMNL ACVLMKMNMN
ESLVAATLNA AASINKSSTH GSLEVGKFAD FVILSADKWE HIIYEMVDPP ISHVFKKGNL
VFSNNN
