HUTI_MOUSE
ID HUTI_MOUSE Reviewed; 426 AA.
AC Q9DBA8; Q7TPP5; Q811K3; Q8R230;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable imidazolonepropionase;
DE EC=3.5.2.7;
DE AltName: Full=Amidohydrolase domain-containing protein 1;
GN Name=Amdhd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK005066; BAB23790.1; -; mRNA.
DR EMBL; BC022626; AAH22626.1; -; mRNA.
DR EMBL; BC043681; AAH43681.1; -; mRNA.
DR EMBL; BC055025; AAH55025.1; -; mRNA.
DR EMBL; BC118616; AAI18617.1; -; mRNA.
DR EMBL; BC121826; AAI21827.1; -; mRNA.
DR CCDS; CCDS48671.1; -.
DR RefSeq; NP_082184.1; NM_027908.1.
DR AlphaFoldDB; Q9DBA8; -.
DR SMR; Q9DBA8; -.
DR STRING; 10090.ENSMUSP00000016034; -.
DR MEROPS; M38.980; -.
DR iPTMnet; Q9DBA8; -.
DR PhosphoSitePlus; Q9DBA8; -.
DR SwissPalm; Q9DBA8; -.
DR jPOST; Q9DBA8; -.
DR MaxQB; Q9DBA8; -.
DR PaxDb; Q9DBA8; -.
DR PeptideAtlas; Q9DBA8; -.
DR PRIDE; Q9DBA8; -.
DR ProteomicsDB; 273207; -.
DR Antibodypedia; 30145; 125 antibodies from 19 providers.
DR DNASU; 71761; -.
DR Ensembl; ENSMUST00000016034; ENSMUSP00000016034; ENSMUSG00000015890.
DR GeneID; 71761; -.
DR KEGG; mmu:71761; -.
DR UCSC; uc007gut.2; mouse.
DR CTD; 144193; -.
DR MGI; MGI:1919011; Amdhd1.
DR VEuPathDB; HostDB:ENSMUSG00000015890; -.
DR eggNOG; KOG3968; Eukaryota.
DR GeneTree; ENSGT00390000008645; -.
DR HOGENOM; CLU_041647_2_0_1; -.
DR InParanoid; Q9DBA8; -.
DR OMA; CAPHARW; -.
DR OrthoDB; 776380at2759; -.
DR PhylomeDB; Q9DBA8; -.
DR TreeFam; TF312878; -.
DR Reactome; R-MMU-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00551.
DR BioGRID-ORCS; 71761; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Amdhd1; mouse.
DR PRO; PR:Q9DBA8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DBA8; protein.
DR Bgee; ENSMUSG00000015890; Expressed in left lobe of liver and 20 other tissues.
DR Genevisible; Q9DBA8; MM.
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; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01224; hutI; 1.
PE 1: Evidence at protein level;
KW Histidine metabolism; Hydrolase; Iron; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..426
FT /note="Probable imidazolonepropionase"
FT /id="PRO_0000282583"
FT BINDING 159
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000250|UniProtKB:P42084"
FT BINDING 159
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; 46489 MW; 12C64B2322C106CE CRC64;
MTSSHRLLLE NAQQVVLVCA RGERFLTGSA LRSLAVLEGA SVVVGTDGLI KAVGPAAVIQ
KQFSGETFEE RIDCSGKCVL PGLVDAHTHP VWAGERVHEF AMKLAGATYM DIHQAGGGIN
FTVEHTRQAS EEELFCSFQQ RLQCMMRAGT TLVECKSGYG LNLETELKML RVIERARREL
HLSLSATYCG AHSVPKGKTA VEAADDIISH HLPRLKELSR NGDLHVDNID VFCEKGVFDL
DTTRRILEGG KKMGLQINFH GDELHPMKAA ELGAELGAQA ISHLEEVSDE GIAAMAAARC
SAVLLPTTAY MLRLKQPRAR KMLDEGVIVA LGSDFNPNAY CFSMPMVMHL ACVNMRMSMP
EALAAATINA AYALGKSHTH GSLEVGKQGD AIIINASRWE HLIYQFGGHH ELIDYVITKG
KVIYKK
