Search Results
Overview
| Uniprot ID | A0A4X1SHD1 |
|---|---|
| Protein Name | Porphobilinogen deaminase |
| Gene Name | HMBS |
| Organism | Sus scrofa |
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. 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
MSGNGNAAAT
20
AEENSPKMRV
30
IRVGTRKSQL
40
ARIQTDSVVA
50
TLKALYPGLQ
60
FEIIAMSTTG
70
DKILDTALSK
80
IGEKSLFTKE
90
LEHALERNEV
100
DLVVHSLKDL
110
PTVLPPGFTI
120
GAVCKRECPY
130
DAVVFHPKFV
140
GKTLETLPEK
150
SVVGTSSLRR
160
AAQLQRKFPH
170
LEFKSIRGNL
180
NTRLRKLDEL
190
QEFSAIILAA
200
AGLQRMGWQN
210
RVGQILHPEE
220
CMYAVGQEGG
230
CSVPVAVHTA
240
MKDGQLYLTG
250
GVWSLNGAES
260
MQETMQATIH
270
VPAQHEDGPE
280
DDPQLVGITA
290
RNIPREAQLA
300
AENLGISLAT
310
LLLNKGAKNI
320
LDVARQLNDA
H
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Molecular Function | GO:0004418 | hydroxymethylbilane synthase activity |
| Biological Process | GO:0006783 | heme 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.