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Overview

Uniprot ID	P08397
Protein Name	Porphobilinogen deaminase
Gene Name	HMBS
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
70	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 (PubMed:18004775, PubMed:18936296, PubMed:19138865, PubMed:23815679). 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 (PubMed:18936296). In the last step of catalysis, the product, preuroporphyrinogen, is released, leaving the cofactor bound to the holodeaminase intact (PubMed:18936296)

Protein Sequence

10 MSGNGNAAAT 20 AEENSPKMRV 30 IRVGTRKSQL 40 ARIQTDSVVA 50 TLKASYPGLQ 60 FEIIAMSTTG 70 DKILDTALSK 80 IGEKSLFTKE 90 LEHALEKNEV 100 DLVVHSLKDL 110 PTVLPPGFTI 120 GAICKRENPH 130 DAVVFHPKFV 140 GKTLETLPEK 150 SVVGTSSLRR 160 AAQLQRKFPH 170 LEFRSIRGNL 180 NTRLRKLDEQ 190 QEFSAIILAT 200 AGLQRMGWHN 210 RVGQILHPEE 220 CMYAVGQGAL 230 GVEVRAKDQD 240 ILDLVGVLHD 250 PETLLRCIAE 260 RAFLRHLEGG 270 CSVPVAVHTA 280 MKDGQLYLTG 290 GVWSLDGSDS 300 IQETMQATIH 310 VPAQHEDGPE 320 DDPQLVGITA 330 RNIPRGPQLA 340 AQNLGISLAN 350 LLLSKGAKNI 360 LDVARQLNDA H

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Molecular Function	GO:0004418	hydroxymethylbilane synthase activity
Biological Process	GO:0006784	heme A biosynthetic process
Biological Process	GO:0006785	heme B biosynthetic process
Biological Process	GO:0006783	heme biosynthetic process
Biological Process	GO:0006782	protoporphyrinogen IX biosynthetic process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.