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Protein

Porphobilinogen deaminase

Gene

Hmbs

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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

GO - Molecular functioni

  1. hydroxymethylbilane synthase activity Source: MGI

GO - Biological processi

  1. peptidyl-pyrromethane cofactor linkage Source: InterPro
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Enzyme and pathway databases

BRENDAi2.5.1.61. 3474.
ReactomeiREACT_290357. Heme biosynthesis.
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
Synonyms:Uros1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:96112. Hmbs.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 361360Porphobilinogen deaminasePRO_0000143035Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei74 – 741N6-acetyllysine1 Publication
Modified residuei261 – 2611S-(dipyrrolylmethanemethyl)cysteineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22907.
PaxDbiP22907.
PRIDEiP22907.

Expressioni

Gene expression databases

BgeeiP22907.
CleanExiMM_HMBS.
ExpressionAtlasiP22907. baseline and differential.
GenevestigatoriP22907.

Interactioni

Protein-protein interaction databases

BioGridi200321. 2 interactions.
IntActiP22907. 1 interaction.
MINTiMINT-4097350.

Structurei

3D structure databases

ProteinModelPortaliP22907.
SMRiP22907. Positions 18-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HMBS family.Curated

Phylogenomic databases

eggNOGiCOG0181.
GeneTreeiENSGT00390000009083.
HOGENOMiHOG000228587.
HOVERGENiHBG000967.
InParanoidiP22907.
KOiK01749.
OMAiGIECRTD.
OrthoDBiEOG7W41C4.
TreeFamiTF105389.

Family and domain databases

Gene3Di3.30.160.40. 1 hit.
HAMAPiMF_00260. Porphobil_deam.
InterProiIPR000860. 4pyrrol_synth_OHMeBilane_synth.
IPR022419. Porphobilin_deaminase_cofac_BS.
IPR022417. Porphobilin_deaminase_N.
IPR022418. Porphobilinogen_deaminase_C.
[Graphical view]
PANTHERiPTHR11557. PTHR11557. 1 hit.
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: P22907-1) [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 AEENGSKMRV IRVGTRKSQL ARIQTDTVVA MLKALYPGIQ
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 NTRLRKLDEL QEFSAIVLAV AGLQRMGWQN
210 220 230 240 250
RVGQILHPEE CMYAVGQGAL AVEVRAKDQD ILDLVSVLHD 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):39,344
Last modified:July 27, 2011 - v2
Checksum:iF184C439F4F7B55D
GO
Isoform 2 (identifier: P22907-2) [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):37,781
Checksum:i012E4FE8355D775E
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361D → E in AAA39890 (PubMed:2768242).Curated
Sequence conflicti36 – 361D → E in AAA39891 (PubMed:2768242).Curated
Sequence conflicti64 – 641L → V in AAA39890 (PubMed:2768242).Curated
Sequence conflicti64 – 641L → V in AAA39891 (PubMed:2768242).Curated
Sequence conflicti117 – 1171E → Q in AAA39890 (PubMed:2768242).Curated
Sequence conflicti117 – 1171E → Q in AAA39891 (PubMed:2768242).Curated
Sequence conflicti160 – 1601H → N in AAA39890 (PubMed:2768242).Curated
Sequence conflicti160 – 1601H → N in AAA39891 (PubMed:2768242).Curated
Sequence conflicti271 – 2711M → I in AAA39890 (PubMed:2768242).Curated
Sequence conflicti271 – 2711M → I in AAA39891 (PubMed:2768242).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform 2. CuratedVSP_002068Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28666
, M28663, M28664, M28665 Genomic DNA. Translation: AAA39890.1. Sequence problems.
M28666
, M28663, M28664, M28665 Genomic DNA. Translation: AAA39891.1.
AK166734 mRNA. Translation: BAE38979.1.
AK167702 mRNA. Translation: BAE39746.1.
CCDSiCCDS23106.1. [P22907-1]
CCDS52779.1. [P22907-2]
PIRiA36513. IBMSN.
RefSeqiNP_038579.2. NM_013551.2. [P22907-1]
UniGeneiMm.247676.

Genome annotation databases

EnsembliENSMUST00000077353; ENSMUSP00000076575; ENSMUSG00000032126. [P22907-1]
ENSMUST00000097558; ENSMUSP00000095166; ENSMUSG00000032126. [P22907-2]
GeneIDi15288.
KEGGimmu:15288.
UCSCiuc009pcz.2. mouse. [P22907-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28666
, M28663, M28664, M28665 Genomic DNA. Translation: AAA39890.1. Sequence problems.
M28666
, M28663, M28664, M28665 Genomic DNA. Translation: AAA39891.1.
AK166734 mRNA. Translation: BAE38979.1.
AK167702 mRNA. Translation: BAE39746.1.
CCDSiCCDS23106.1. [P22907-1]
CCDS52779.1. [P22907-2]
PIRiA36513. IBMSN.
RefSeqiNP_038579.2. NM_013551.2. [P22907-1]
UniGeneiMm.247676.

3D structure databases

ProteinModelPortaliP22907.
SMRiP22907. Positions 18-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200321. 2 interactions.
IntActiP22907. 1 interaction.
MINTiMINT-4097350.

Proteomic databases

MaxQBiP22907.
PaxDbiP22907.
PRIDEiP22907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077353; ENSMUSP00000076575; ENSMUSG00000032126. [P22907-1]
ENSMUST00000097558; ENSMUSP00000095166; ENSMUSG00000032126. [P22907-2]
GeneIDi15288.
KEGGimmu:15288.
UCSCiuc009pcz.2. mouse. [P22907-1]

Organism-specific databases

CTDi3145.
MGIiMGI:96112. Hmbs.

Phylogenomic databases

eggNOGiCOG0181.
GeneTreeiENSGT00390000009083.
HOGENOMiHOG000228587.
HOVERGENiHBG000967.
InParanoidiP22907.
KOiK01749.
OMAiGIECRTD.
OrthoDBiEOG7W41C4.
TreeFamiTF105389.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00319.
BRENDAi2.5.1.61. 3474.
ReactomeiREACT_290357. Heme biosynthesis.

Miscellaneous databases

NextBioi287927.
PROiP22907.
SOURCEiSearch...

Gene expression databases

BgeeiP22907.
CleanExiMM_HMBS.
ExpressionAtlasiP22907. baseline and differential.
GenevestigatoriP22907.

Family and domain databases

Gene3Di3.30.160.40. 1 hit.
HAMAPiMF_00260. Porphobil_deam.
InterProiIPR000860. 4pyrrol_synth_OHMeBilane_synth.
IPR022419. Porphobilin_deaminase_cofac_BS.
IPR022417. Porphobilin_deaminase_N.
IPR022418. Porphobilinogen_deaminase_C.
[Graphical view]
PANTHERiPTHR11557. PTHR11557. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  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(1988) [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.
    , 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(2004) [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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHEM3_MOUSE
AccessioniPrimary (citable) accession number: P22907
Secondary accession number(s): Q3TIV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 133 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.