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Protein

5-oxoprolinase

Gene

OPLAH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of 5-oxo-L-proline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.

Catalytic activityi

ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate.

GO - Molecular functioni

  1. 5-oxoprolinase (ATP-hydrolyzing) activity Source: Reactome
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. glutathione biosynthetic process Source: Reactome
  2. glutathione derivative biosynthetic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
  4. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_6960. Glutathione synthesis and recycling.

Names & Taxonomyi

Protein namesi
Recommended name:
5-oxoprolinase (EC:3.5.2.9)
Alternative name(s):
5-oxo-L-prolinase
Short name:
5-OPase
Pyroglutamase
Gene namesi
Name:OPLAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:8149. OPLAH.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

5-oxoprolinase deficiency1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by calcium oxalate/carbonate urolithiasis, and excessive urinary 5-oxo-L-proline. Affected individuals have recurrent episodes of vomiting, diarrhea, and abdominal pain.

See also OMIM:260005

Organism-specific databases

MIMi260005. phenotype.
Orphaneti33572. 5-oxoprolinase deficiency.
PharmGKBiPA31935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128812885-oxoprolinasePRO_0000208577Add
BLAST

Proteomic databases

MaxQBiO14841.
PaxDbiO14841.
PRIDEiO14841.

PTM databases

PhosphoSiteiO14841.

Expressioni

Gene expression databases

CleanExiHS_OPLAH.
GenevestigatoriO14841.

Organism-specific databases

HPAiHPA026562.
HPA028260.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi117922. 3 interactions.
IntActiO14841. 1 interaction.
STRINGi9606.ENSP00000412071.

Structurei

3D structure databases

ProteinModelPortaliO14841.
SMRiO14841. Positions 450-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the oxoprolinase family.Curated

Phylogenomic databases

eggNOGiCOG0146.
GeneTreeiENSGT00390000013463.
HOGENOMiHOG000047200.
HOVERGENiHBG007870.
InParanoidiO14841.
KOiK01469.
OMAiGNARMGY.
PhylomeDBiO14841.

Family and domain databases

InterProiIPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view]
PfamiPF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSPEGRFHF AIDRGGTFTD VFAQCPGGHV RVLKLLSEDP ANYADAPTEG
60 70 80 90 100
IRRILEQEAG MLLPRDQPLD SSHIASIRMG TTVATNALLE RKGERVALLV
110 120 130 140 150
TRGFRDLLHI GTQARGDLFD LAVPMPEVLY EEVLEVDERV VLHRGEAGTG
160 170 180 190 200
TPVKGRTGDL LEVQQPVDLG ALRGKLEGLL SRGIRSLAVV LMHSYTWAQH
210 220 230 240 250
EQQVGVLARE LGFTHVSLSS EAMPMVRIVP RGHTACADAY LTPAIQRYVQ
260 270 280 290 300
GFCRGFQGQL KDVQVLFMRS DGGLAPMDTF SGSSAVLSGP AGGVVGYSAT
310 320 330 340 350
TYQQEGGQPV IGFDMGGTST DVSRYAGEFE HVFEASTAGV TLQAPQLDIN
360 370 380 390 400
TVAAGGGSRL FFRSGLFVVG PESAGAHPGP ACYRKGGPVT VTDANLVLGR
410 420 430 440 450
LLPASFPCIF GPGENQPLSP EASRKALEAV ATEVNSFLTN GPCPASPLSL
460 470 480 490 500
EEVAMGFVRV ANEAMCRPIR ALTQARGHDP SAHVLACFGG AGGQHACAIA
510 520 530 540 550
RALGMDTVHI HRHSGLLSAL GLALADVVHE AQEPCSLLYA PETFVQLDQR
560 570 580 590 600
LSRLEEQCVD ALQAQGFPRS QISTESFLHL RYQGTDCALM VSAHQHPATA
610 620 630 640 650
RSPRAGDFGA AFVERYMREF GFVIPERPVV VDDVRVRGTG RSGLRLEDAP
660 670 680 690 700
KAQTGPPRVD KMTQCYFEGG YQETPVYLLA ELGYGHKLHG PCLIIDSNST
710 720 730 740 750
ILVEPGCQAE VTKTGDICIS VGAEVPGTVG PQLDPIQLSI FSHRFMSIAE
760 770 780 790 800
QMGRILQRTA ISTNIKERLD FSCALFGPDG GLVSNAPHIP VHLGAMQETV
810 820 830 840 850
QFQIQHLGAD LHPGDVLLSN HPSAGGSHLP DLTVITPVFW PGQTRPVFYV
860 870 880 890 900
ASRGHHADIG GITPGSMPPH STMLQQEGAV FLSFKLVQGG VFQEEAVTEA
910 920 930 940 950
LRAPGKVPNC SGTRNLHDNL SDLRAQVAAN QKGIQLVGEL IGQYGLDVVQ
960 970 980 990 1000
AYMGHIQANA ELAVRDMLRA FGTSRQARGL PLEVSSEDHM DDGSPIRLRV
1010 1020 1030 1040 1050
QISLSQGSAV FDFSGTGPEV FGNLNAPRAV TLSALIYCLR CLVGRDIPLN
1060 1070 1080 1090 1100
QGCLAPVRVV IPRGSILDPS PEAAVVGGNV LTSQRVVDVI LGAFGACAAS
1110 1120 1130 1140 1150
QGCMNNVTLG NAHMGYYETV AGGAGAGPSW HGRSGVHSHM TNTRITDPEI
1160 1170 1180 1190 1200
LESRYPVILR RFELRRGSGG RGRFRGGDGV TRELLFREEA LLSVLTERRA
1210 1220 1230 1240 1250
FRPYGLHGGE PGARGLNLLI RKNGRTVNLG GKTSVTVYPG DVFCLHTPGG
1260 1270 1280
GGYGDPEDPA PPPGSPPQAL AFPEHGSVYE YRRAQEAV
Length:1,288
Mass (Da):137,457
Last modified:February 15, 2005 - v3
Checksum:i999AC0FA497750F2
GO

Sequence cautioni

The sequence AAB81519.1 differs from that shown. Reason: Frameshift at positions 1046, 1068 and 1080. Curated
The sequence CAB46426.2 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1084 – 10896QRVVDV → NAWWMF in AAB81519 (Ref. 4) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti284 – 2841S → R.
Corresponds to variant rs3935209 [ dbSNP | Ensembl ].
VAR_050425

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB122018 mRNA. Translation: BAD13434.1.
BC142672 mRNA. Translation: AAI42673.1.
AL096750 mRNA. Translation: CAB46426.2. Frameshift.
AH005594 Genomic DNA. Translation: AAB81519.1. Frameshift.
CCDSiCCDS75802.1.
PIRiT12537.
RefSeqiNP_060040.1. NM_017570.4.
UniGeneiHs.305882.

Genome annotation databases

EnsembliENST00000618853; ENSP00000480476; ENSG00000178814.
GeneIDi26873.
KEGGihsa:26873.
UCSCiuc003zar.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB122018 mRNA. Translation: BAD13434.1.
BC142672 mRNA. Translation: AAI42673.1.
AL096750 mRNA. Translation: CAB46426.2. Frameshift.
AH005594 Genomic DNA. Translation: AAB81519.1. Frameshift.
CCDSiCCDS75802.1.
PIRiT12537.
RefSeqiNP_060040.1. NM_017570.4.
UniGeneiHs.305882.

3D structure databases

ProteinModelPortaliO14841.
SMRiO14841. Positions 450-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117922. 3 interactions.
IntActiO14841. 1 interaction.
STRINGi9606.ENSP00000412071.

PTM databases

PhosphoSiteiO14841.

Proteomic databases

MaxQBiO14841.
PaxDbiO14841.
PRIDEiO14841.

Protocols and materials databases

DNASUi26873.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000618853; ENSP00000480476; ENSG00000178814.
GeneIDi26873.
KEGGihsa:26873.
UCSCiuc003zar.3. human.

Organism-specific databases

CTDi26873.
GeneCardsiGC08M145106.
HGNCiHGNC:8149. OPLAH.
HPAiHPA026562.
HPA028260.
MIMi260005. phenotype.
614243. gene.
neXtProtiNX_O14841.
Orphaneti33572. 5-oxoprolinase deficiency.
PharmGKBiPA31935.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0146.
GeneTreeiENSGT00390000013463.
HOGENOMiHOG000047200.
HOVERGENiHBG007870.
InParanoidiO14841.
KOiK01469.
OMAiGNARMGY.
PhylomeDBiO14841.

Enzyme and pathway databases

ReactomeiREACT_6960. Glutathione synthesis and recycling.

Miscellaneous databases

GenomeRNAii26873.
NextBioi49396.
PROiO14841.
SOURCEiSearch...

Gene expression databases

CleanExiHS_OPLAH.
GenevestigatoriO14841.

Family and domain databases

InterProiIPR008040. Hydant_A_N.
IPR002821. Hydantoinase_A.
IPR003692. Hydantoinase_B.
[Graphical view]
PfamiPF05378. Hydant_A_N. 1 hit.
PF01968. Hydantoinase_A. 1 hit.
PF02538. Hydantoinase_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bovine 5-oxo-L-prolinase: simple assay method, purification, cDNA cloning, and detection of mRNA in the coronary artery."
    Watanabe T., Abe K., Ishikawa H., Iijima Y.
    Biol. Pharm. Bull. 27:288-294(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-1288.
    Tissue: Testis.
  4. "Human 5-oxo-L-prolinase partial sequence."
    Debella L.R., Wood S.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 901-1096.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "5-Oxoprolinase deficiency: report of the first human OPLAH mutation."
    Almaghlouth I., Mohamed J., Al-Amoudi M., Al-Ahaidib L., Al-Odaib A., Alkuraya F.
    Clin. Genet. 82:193-196(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN OPLAHD.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiOPLA_HUMAN
AccessioniPrimary (citable) accession number: O14841
Secondary accession number(s): A5PKY8, Q75W65, Q9Y4Q0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 15, 2005
Last modified: March 4, 2015
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.