Search Results
Overview
| Uniprot ID | A0A8W4FLX8 |
|---|---|
| Protein Name | Porphobilinogen deaminase |
| Gene Name | HMBS |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 62 | 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
FLQEENSPKM
20
RVIRVGTRKS
30
QLARIQTDSV
40
VATLKALYPG
50
LQFEIIAMST
60
TGDKILDTAL
70
SKIGEKSLFT
80
KELEHALERN
90
EVDLVVHSLK
100
DLPTVLPPGF
110
TIGAVCKREC
120
PYDAVVFHPK
130
FVGKTLETLP
140
EKSVVGTSSL
150
RRAAQLQRKF
160
PHLEFKSIRG
170
NLNTRLRKLD
180
ELQEFSAIIL
190
AAAGLQRMGW
200
QNRVGQILHP
210
EECMYAVGQG
220
ALGVEVRAKD
230
QDILDLVGVL
240
HDPETLLRCI
250
AERAFLRHLE
260
GGCSVPVAVH
270
TAMKDGQLYL
280
TGGVWSLNGA
290
ESMQETMQAT
300
IHVPAQHEDG
310
PEDDPQLVGI
320
TARNIPREAQ
330
LAAENLGISL
340
ATLLLNKGAK
350
NILDVARQLN
DAH
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Biological Process | GO:0006783 | heme biosynthetic process |
| Molecular Function | GO:0004418 | hydroxymethylbilane synthase activity |
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.