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Overview

Uniprot IDA0A287B3J0
Protein NamePorphobilinogen deaminase
Gene NameHMBS
OrganismSus scrofa

Kla Sites from experimental identification

Position Flanking peptide
53 ILDTALSKIGEKSLF

Function

As part of the heme biosynthetic pathway, catalyzes the sequential polymerization of four molecules of porphobilinogen to form hydroxymethylbilane, also known as preuroporphyrinogen. Catalysis begins with the assembly of the dipyrromethane cofactor by the apoenzyme from two molecules of porphobilinogen or from preuroporphyrinogen. The covalently linked cofactor acts as a primer, around which the tetrapyrrole product is assembled. In the last step of catalysis, the product, preuroporphyrinogen, is released, leaving the cofactor bound to the holodeaminase intact

Protein Sequence

10 MRVIRVGTRK 20 SQLARIQTDS 30 VVATLKALYP 40 GLQFEIIAMS 50 TTGDKILDTA 60 LSKIGEKSLF 70 TKELEHALER 80 NEVDLVVHSL 90 KDLPTVLPPG 100 FTIGAVCKRE 110 CPYDAVVFHP 120 KFVGKTLETL 130 PEKSVVGTSS 140 LRRAAQLQRK 150 FPHLEFKSIR 160 GNLNTRLRKL 170 DELQEFSAII 180 LAAAGLQRMG 190 WQNRVGQILH 200 PEECMYAVGQ 210 GALGVEVRAK 220 DQDILDLVGV 230 LHDPETLLRC 240 IAERAFLRHL 250 EGGCSVPVAV 260 HTAMKDGQLY 270 LTGGVWSLNG 280 AESMQETMQA 290 TIHVPAQHED 300 GPEDDPQLVG 310 ITARNIPREA 320 QLAAENLGIS 330 LATLLLNKGA 340 KNILDVARQL NDAH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Molecular Function GO:0004418 hydroxymethylbilane synthase activity
Biological Process GO:0006782 protoporphyrinogen IX biosynthetic process

Reference

[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.