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Protein

Porphobilinogen deaminase

Gene

Hmbs

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.

Catalytic activityi

4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3.

Cofactori

dipyrromethaneNote: Binds 1 dipyrromethane group covalently.

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (Alad)
  2. Porphobilinogen deaminase (Hmbs)
  3. no protein annotated in this organism
  4. Uroporphyrinogen decarboxylase (Urod), Uroporphyrinogen decarboxylase (Urod)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

  • amine binding Source: RGD
  • carboxylic acid binding Source: RGD
  • coenzyme binding Source: RGD
  • hydroxymethylbilane synthase activity Source: RGD
  • uroporphyrinogen-III synthase activity Source: RGD

GO - Biological processi

  • animal organ regeneration Source: RGD
  • astrocyte differentiation Source: RGD
  • cellular response to amine stimulus Source: RGD
  • cellular response to antibiotic Source: RGD
  • cellular response to arsenic-containing substance Source: RGD
  • cellular response to cytokine stimulus Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to lead ion Source: RGD
  • heme biosynthetic process Source: GO_Central
  • peptidyl-pyrromethane cofactor linkage Source: InterPro
  • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  • response to amino acid Source: RGD
  • response to carbohydrate Source: RGD
  • response to cobalt ion Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
  • response to lead ion Source: RGD
  • response to metal ion Source: RGD
  • response to methylmercury Source: RGD
  • response to nutrient levels Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to vitamin Source: RGD
  • response to zinc ion Source: RGD
  • tetrapyrrole biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Enzyme and pathway databases

BRENDAi2.5.1.61. 5301.
SABIO-RKP19356.
UniPathwayiUPA00251; UER00319.

Names & Taxonomyi

Protein namesi
Recommended name:
Porphobilinogen deaminase (EC:2.5.1.61)
Short name:
PBG-D
Alternative name(s):
Hydroxymethylbilane synthase
Short name:
HMBS
Pre-uroporphyrinogen synthase
Gene namesi
Name:Hmbs
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2801. Hmbs.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001430362 – 361Porphobilinogen deaminaseAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei69PhosphoserineBy similarity1
Modified residuei74N6-acetyllysineBy similarity1
Modified residuei147PhosphoserineBy similarity1
Modified residuei261S-(dipyrrolylmethanemethyl)cysteineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP19356.
PRIDEiP19356.

PTM databases

iPTMnetiP19356.
PhosphoSitePlusiP19356.
SwissPalmiP19356.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014128.

Structurei

3D structure databases

ProteinModelPortaliP19356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HMBS family.Curated

Phylogenomic databases

eggNOGiKOG2892. Eukaryota.
COG0181. LUCA.
HOGENOMiHOG000228587.
HOVERGENiHBG000967.
InParanoidiP19356.
PhylomeDBiP19356.

Family and domain databases

Gene3Di3.30.160.40. 1 hit.
HAMAPiMF_00260. Porphobil_deam. 1 hit.
InterProiIPR000860. HemC.
IPR022419. Porphobilin_deaminase_cofac_BS.
IPR022417. Porphobilin_deaminase_N.
IPR022418. Porphobilinogen_deaminase_C.
[Graphical view]
PANTHERiPTHR11557. PTHR11557. 2 hits.
PfamiPF01379. Porphobil_deam. 1 hit.
PF03900. Porphobil_deamC. 1 hit.
[Graphical view]
PIRSFiPIRSF001438. 4pyrrol_synth_OHMeBilane_synth. 1 hit.
PRINTSiPR00151. PORPHBDMNASE.
SUPFAMiSSF54782. SSF54782. 2 hits.
TIGRFAMsiTIGR00212. hemC. 1 hit.
PROSITEiPS00533. PORPHOBILINOGEN_DEAM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19356-1) [UniParc]FASTAAdd to basket
Also known as: Non-erythropoietic

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGNGGAATT AEENGSMMRV IRVGTRKSQL ARIQTDTVVA MLKTLYPGIQ
60 70 80 90 100
FEIIAMSTTG DKILDTALSK IGEKSLFTKE LENALEKNEV DLVVHSLKDV
110 120 130 140 150
PTILPPGFTI GAICKRENPC DAVVFHPKFI GKTLETLPEK SAVGTSSLRR
160 170 180 190 200
VAQLQRKFPH LEFKSIRGNL NTRLRKLDEQ LEFSAIILAV AGLQRMGWQN
210 220 230 240 250
RVGQILHPEE CMYAVGQGAL AVEVRAKDQD ILDLVGVLHD PETLLRCIAE
260 270 280 290 300
RAFLRHLEGG CSVPVAVHTV MKDGQLYLTG GVWSLDGSDS MQETMQATIQ
310 320 330 340 350
VPVQQEDGPE DDPQLVGITA RNIPRGAQLA AENLGISLAS LLLNKGAKNI
360
LDVARQLNDV R
Length:361
Mass (Da):39,361
Last modified:November 1, 1997 - v2
Checksum:iCE00570010E4121E
GO
Isoform 2 (identifier: P19356-2) [UniParc]FASTAAdd to basket
Also known as: Erythrocyte

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Show »
Length:344
Mass (Da):37,795
Checksum:i1EF0BC882AA8F5F9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti126 – 127HP → EG in CAA29984 (PubMed:3368319).Curated2
Sequence conflicti252A → D in CAA29984 (PubMed:3368319).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0020691 – 17Missing in isoform 2. 1 PublicationAdd BLAST17

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06827 mRNA. Translation: CAA29984.1.
Y12006 mRNA. Translation: CAA72734.1.
PIRiJE0285. IBRTE.
UniGeneiRn.11080.

Genome annotation databases

UCSCiRGD:2801. rat. [P19356-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06827 mRNA. Translation: CAA29984.1.
Y12006 mRNA. Translation: CAA72734.1.
PIRiJE0285. IBRTE.
UniGeneiRn.11080.

3D structure databases

ProteinModelPortaliP19356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014128.

PTM databases

iPTMnetiP19356.
PhosphoSitePlusiP19356.
SwissPalmiP19356.

Proteomic databases

PaxDbiP19356.
PRIDEiP19356.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2801. rat. [P19356-1]

Organism-specific databases

RGDi2801. Hmbs.

Phylogenomic databases

eggNOGiKOG2892. Eukaryota.
COG0181. LUCA.
HOGENOMiHOG000228587.
HOVERGENiHBG000967.
InParanoidiP19356.
PhylomeDBiP19356.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00319.
BRENDAi2.5.1.61. 5301.
SABIO-RKP19356.

Miscellaneous databases

PROiP19356.

Family and domain databases

Gene3Di3.30.160.40. 1 hit.
HAMAPiMF_00260. Porphobil_deam. 1 hit.
InterProiIPR000860. HemC.
IPR022419. Porphobilin_deaminase_cofac_BS.
IPR022417. Porphobilin_deaminase_N.
IPR022418. Porphobilinogen_deaminase_C.
[Graphical view]
PANTHERiPTHR11557. PTHR11557. 2 hits.
PfamiPF01379. Porphobil_deam. 1 hit.
PF03900. Porphobil_deamC. 1 hit.
[Graphical view]
PIRSFiPIRSF001438. 4pyrrol_synth_OHMeBilane_synth. 1 hit.
PRINTSiPR00151. PORPHBDMNASE.
SUPFAMiSSF54782. SSF54782. 2 hits.
TIGRFAMsiTIGR00212. hemC. 1 hit.
PROSITEiPS00533. PORPHOBILINOGEN_DEAM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM3_RAT
AccessioniPrimary (citable) accession number: P19356
Secondary accession number(s): O08568
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The porphobilinogen subunits are added to the dipyrromethane group.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.