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P22907 (HEM3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Porphobilinogen deaminase

Short name=PBG-D
EC=2.5.1.61
Alternative name(s):
Hydroxymethylbilane synthase
Short name=HMBS
Pre-uroporphyrinogen synthase
Gene names
Name:Hmbs
Synonyms:Uros1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. HAMAP-Rule MF_00260

Catalytic activity

4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3. HAMAP-Rule MF_00260

Cofactor

Binds 1 dipyrromethane group covalently.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4. HAMAP-Rule MF_00260

Miscellaneous

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

Sequence similarities

Belongs to the HMBS family.

Sequence caution

The sequence AAA39890.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Coding sequence diversityAlternative splicing
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-pyrromethane cofactor linkage

Inferred from electronic annotation. Source: InterPro

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionhydroxymethylbilane synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22907-1)

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.
Isoform 2 (identifier: P22907-2)

Also known as: Erythrocyte;

The sequence of this isoform differs from the canonical sequence as follows:
     2-17: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 361360Porphobilinogen deaminase HAMAP-Rule MF_00260
PRO_0000143035

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue741N6-acetyllysine Ref.3
Modified residue2611S-(dipyrrolylmethanemethyl)cysteine By similarity

Natural variations

Alternative sequence2 – 1716Missing in isoform 2.
VSP_002068

Experimental info

Sequence conflict361D → E in AAA39890. Ref.1
Sequence conflict361D → E in AAA39891. Ref.1
Sequence conflict641L → V in AAA39890. Ref.1
Sequence conflict641L → V in AAA39891. Ref.1
Sequence conflict1171E → Q in AAA39890. Ref.1
Sequence conflict1171E → Q in AAA39891. Ref.1
Sequence conflict1601H → N in AAA39890. Ref.1
Sequence conflict1601H → N in AAA39891. Ref.1
Sequence conflict2711M → I in AAA39890. Ref.1
Sequence conflict2711M → I in AAA39891. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Non-erythropoietic) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F184C439F4F7B55D

FASTA36139,344
        10         20         30         40         50         60 
MSGNGGAATT AEENGSKMRV IRVGTRKSQL ARIQTDTVVA MLKALYPGIQ FEIIAMSTTG 

        70         80         90        100        110        120 
DKILDTALSK IGEKSLFTKE LENALEKNEV DLVVHSLKDV PTILPPGFTI GAICKRENPC 

       130        140        150        160        170        180 
DAVVFHPKFI GKTLETLPEK SAVGTSSLRR VAQLQRKFPH LEFKSIRGNL NTRLRKLDEL 

       190        200        210        220        230        240 
QEFSAIVLAV AGLQRMGWQN RVGQILHPEE CMYAVGQGAL AVEVRAKDQD ILDLVSVLHD 

       250        260        270        280        290        300 
PETLLRCIAE RAFLRHLEGG CSVPVAVHTV MKDGQLYLTG GVWSLDGSDS MQETMQATIQ 

       310        320        330        340        350        360 
VPVQQEDGPE DDPQLVGITA RNIPRGAQLA AENLGISLAS LLLNKGAKNI LDVARQLNDV 


R 

« Hide

Isoform 2 (Erythrocyte) [UniParc].

Checksum: D74599AABD83A6BA
Show »

FASTA34537,912

References

« Hide 'large scale' references
[1]"The mouse porphobilinogen deaminase gene. Structural organization, sequence, and transcriptional analysis."
Beaumont C., Porcher C., Picat C., Nordmann Y., Grandchamp B.
J. Biol. Chem. 264:14829-14834(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Amnion.
[3]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28666 expand/collapse EMBL AC list , M28663, M28664, M28665 Genomic DNA. Translation: AAA39890.1. Sequence problems.
M28666 expand/collapse EMBL AC list , M28663, M28664, M28665 Genomic DNA. Translation: AAA39891.1.
AK166734 mRNA. Translation: BAE38979.1.
AK167702 mRNA. Translation: BAE39746.1.
CCDSCCDS23106.1. [P22907-1]
CCDS52779.1. [P22907-2]
PIRIBMSN. A36513.
RefSeqNP_038579.2. NM_013551.2. [P22907-1]
UniGeneMm.247676.

3D structure databases

ProteinModelPortalP22907.
SMRP22907. Positions 18-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200321. 1 interaction.
IntActP22907. 1 interaction.
MINTMINT-4097350.

Proteomic databases

PaxDbP22907.
PRIDEP22907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000077353; ENSMUSP00000076575; ENSMUSG00000032126. [P22907-1]
GeneID15288.
KEGGmmu:15288.
UCSCuc009pcz.2. mouse. [P22907-1]

Organism-specific databases

CTD3145.
MGIMGI:96112. Hmbs.

Phylogenomic databases

eggNOGCOG0181.
GeneTreeENSGT00390000009083.
HOGENOMHOG000228587.
HOVERGENHBG000967.
InParanoidQ3TIV0.
KOK01749.
OMAGIECRTD.
OrthoDBEOG7W41C4.
TreeFamTF105389.

Enzyme and pathway databases

UniPathwayUPA00251; UER00319.

Gene expression databases

ArrayExpressP22907.
BgeeP22907.
CleanExMM_HMBS.
GenevestigatorP22907.

Family and domain databases

Gene3D3.30.160.40. 1 hit.
HAMAPMF_00260. Porphobil_deam.
InterProIPR000860. 4pyrrol_synth_OHMeBilane_synth.
IPR022419. Porphobilin_deaminase_cofac_BS.
IPR022417. Porphobilin_deaminase_N.
IPR022418. Porphobilinogen_deaminase_C.
[Graphical view]
PANTHERPTHR11557. PTHR11557. 1 hit.
PfamPF01379. Porphobil_deam. 1 hit.
PF03900. Porphobil_deamC. 1 hit.
[Graphical view]
PIRSFPIRSF001438. 4pyrrol_synth_OHMeBilane_synth. 1 hit.
PRINTSPR00151. PORPHBDMNASE.
SUPFAMSSF54782. SSF54782. 2 hits.
TIGRFAMsTIGR00212. hemC. 1 hit.
PROSITEPS00533. PORPHOBILINOGEN_DEAM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287927.
PROP22907.
SOURCESearch...

Entry information

Entry nameHEM3_MOUSE
AccessionPrimary (citable) accession number: P22907
Secondary accession number(s): Q3TIV0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot