Overview
| Uniprot ID | Q96NU7 |
| Protein Name | Probable imidazolonepropionase |
| Gene Name | AMDHD1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 214 |
IINNHLPKLKELGRN |
Function
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to form N-formimidoyl-L-glutamate. This reaction represents the third step of the universal histidine degradation pathway. In addition to its metabolic role, functions as a tumor suppressor by promoting TGF-beta signaling. Mechanistically, inhibits ubiquitination and proteasomal degradation of SMAD4, thereby stabilizing the protein. Enhances SMAD2/3 phosphorylation and increases TGF-beta-dependent transcriptional responses. Consequently, promotes apoptosis and induces cell cycle arrest in tumor cells (PubMed:39143229)
Protein Sequence
10
MASGHSLLLE
20
NAQQVVLVCA
30
RGERFLARDA
40
LRSLAVLEGA
50
SLVVGKDGFI
60
KAIGPADVIQ
70
RQFSGETFEE
80
IIDCSGKCIL
90
PGLVDAHTHP
100
VWAGERVHEF
110
AMKLAGATYM
120
EIHQAGGGIH
130
FTVERTRQAT
140
EEELFRSLQQ
150
RLQCMMRAGT
160
TLVECKSGYG
170
LDLETELKML
180
RVIERARREL
190
DIGISATYCG
200
AHSVPKGKTA
210
TEAADDIINN
220
HLPKLKELGR
230
NGEIHVDNID
240
VFCEKGVFDL
250
DSTRRILQRG
260
KDIGLQINFH
270
GDELHPMKAA
280
ELGAELGAQA
290
ISHLEEVSDE
300
GIVAMATARC
310
SAILLPTTAY
320
MLRLKQPRAR
330
KMLDEGVIVA
340
LGSDFNPNAY
350
CFSMPMVMHL
360
ACVNMRMSMP
370
EALAAATINA
380
AYALGKSHTH
390
GSLEVGKQGD
400
LIIINSSRWE
410
HLIYQFGGHH
420
ELIEYVIAKG
KLIYKT
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005829 |
cytosol |
| Molecular Function |
GO:0016812 |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| Molecular Function |
GO:0050480 |
imidazolonepropionase activity |
| Molecular Function |
GO:0046872 |
metal ion binding |
| Biological Process |
GO:0006548 |
L-histidine catabolic process |
| Biological Process |
GO:0019556 |
L-histidine catabolic process to glutamate and formamide |
| Biological Process |
GO:0019557 |
L-histidine catabolic process to glutamate and formate |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.