Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trans-3-hydroxy-L-proline dehydratase

Gene

L3HYPDH

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

Functioni

Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it.1 Publication

Catalytic activityi

Trans-3-hydroxy-L-proline = 1-pyrroline 2-carboxylate + H2O.2 Publications

Kineticsi

  1. KM=7.23 mM for trans-3-hydroxy-L-proline1 Publication

Vmax=39.5 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton acceptorBy similarity
Binding sitei269 – 2691SubstrateBy similarity

GO - Molecular functioni

  1. hydro-lyase activity Source: UniProtKB
  2. trans-L-3-hydroxyproline dehydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Names & Taxonomyi

Protein namesi
Recommended name:
Trans-3-hydroxy-L-proline dehydratase2 Publications (EC:4.2.1.772 Publications)
Alternative name(s):
Trans-L-3-hydroxyproline dehydratase
Gene namesi
Name:L3HYPDH
Synonyms:C14orf149
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20488. L3HYPDH.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi273 – 2731T → C: Regains racemase activity, catalyzing the conversion of trans-3-hydroxy-L-proline to cis-3-hydroxy-D-proline. Also catalyzes racemization of L-proline to D-proline, albeit at a very low level. Has lost its original dehydratase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134961537.

Chemistry

DrugBankiDB00172. L-Proline.

Polymorphism and mutation databases

BioMutaiL3HYPDH.
DMDMi296452868.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Trans-3-hydroxy-L-proline dehydratasePRO_0000288949Add
BLAST

Proteomic databases

MaxQBiQ96EM0.
PaxDbiQ96EM0.
PRIDEiQ96EM0.

PTM databases

PhosphoSiteiQ96EM0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ96EM0.
CleanExiHS_C14orf149.
ExpressionAtlasiQ96EM0. baseline and differential.
GenevestigatoriQ96EM0.

Organism-specific databases

HPAiHPA056694.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi125210. 13 interactions.
STRINGi9606.ENSP00000247194.

Structurei

3D structure databases

ProteinModelPortaliQ96EM0.
SMRiQ96EM0. Positions 20-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1062Substrate bindingBy similarity
Regioni274 – 2752Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the proline racemase family.Curated

Phylogenomic databases

eggNOGiCOG3938.
GeneTreeiENSGT00390000002032.
HOGENOMiHOG000084336.
HOVERGENiHBG057443.
InParanoidiQ96EM0.
KOiK18384.
OMAiCPCGLVT.
OrthoDBiEOG75F4DB.
PhylomeDBiQ96EM0.
TreeFamiTF329167.

Family and domain databases

InterProiIPR008794. Pro_racemase_fam.
[Graphical view]
PfamiPF05544. Pro_racemase. 1 hit.
[Graphical view]
PIRSFiPIRSF029792. Pro_racemase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q96EM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESALAVPRL PPHDPGTPVL SVVDMHTGGE PLRIVLAGCP EVSGPTLLAK
60 70 80 90 100
RRYMRQHLDH VRRRLMFEPR GHRDMYGAVL VPSELPDAHL GVLFLHNEGY
110 120 130 140 150
SSMCGHAVLA LGRFALDFGL VPAPPAGTRE ARVNIHCPCG LVTAFVACED
160 170 180 190 200
GRSHGPVRFH SVPAFVLATD LMVDVPGHGK VMVDIAYGGA FYAFVTAEKL
210 220 230 240 250
GLDICSAKTR DLVDAASAVT EAVKAQFKIN HPDSEDLAFL YGTILTDGKD
260 270 280 290 300
AYTKEPTTNI CVFADEQVDR SPTGSGVTAR IALQYHKGLL ELNQMRAFKS
310 320 330 340 350
SATGSVFTGK AVREAKCGDF KAVIVEVSGQ AHYTGTASFI IEDDDPLRDG

FLLK
Length:354
Mass (Da):38,138
Last modified:May 18, 2010 - v2
Checksum:iD279EE0B7C679969
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91R → W in AAH12131 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421V → A.
Corresponds to variant rs17096291 [ dbSNP | Ensembl ].
VAR_032540
Natural varianti125 – 1251P → S.
Corresponds to variant rs35622288 [ dbSNP | Ensembl ].
VAR_062192
Natural varianti315 – 3151A → V.
Corresponds to variant rs1046701 [ dbSNP | Ensembl ].
VAR_032541
Natural varianti341 – 3411I → V.
Corresponds to variant rs8660 [ dbSNP | Ensembl ].
VAR_032542

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK058165 mRNA. Translation: BAB71696.1.
AL159140 Genomic DNA. No translation available.
BC012131 mRNA. Translation: AAH12131.1.
CCDSiCCDS9739.1.
RefSeqiNP_653182.1. NM_144581.1.
UniGeneiHs.729061.

Genome annotation databases

EnsembliENST00000247194; ENSP00000247194; ENSG00000126790.
GeneIDi112849.
KEGGihsa:112849.
UCSCiuc001xee.1. human.

Polymorphism and mutation databases

BioMutaiL3HYPDH.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK058165 mRNA. Translation: BAB71696.1.
AL159140 Genomic DNA. No translation available.
BC012131 mRNA. Translation: AAH12131.1.
CCDSiCCDS9739.1.
RefSeqiNP_653182.1. NM_144581.1.
UniGeneiHs.729061.

3D structure databases

ProteinModelPortaliQ96EM0.
SMRiQ96EM0. Positions 20-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125210. 13 interactions.
STRINGi9606.ENSP00000247194.

Chemistry

DrugBankiDB00172. L-Proline.

PTM databases

PhosphoSiteiQ96EM0.

Polymorphism and mutation databases

BioMutaiL3HYPDH.
DMDMi296452868.

Proteomic databases

MaxQBiQ96EM0.
PaxDbiQ96EM0.
PRIDEiQ96EM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247194; ENSP00000247194; ENSG00000126790.
GeneIDi112849.
KEGGihsa:112849.
UCSCiuc001xee.1. human.

Organism-specific databases

CTDi112849.
GeneCardsiGC14M059928.
HGNCiHGNC:20488. L3HYPDH.
HPAiHPA056694.
MIMi614811. gene.
neXtProtiNX_Q96EM0.
PharmGKBiPA134961537.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3938.
GeneTreeiENSGT00390000002032.
HOGENOMiHOG000084336.
HOVERGENiHBG057443.
InParanoidiQ96EM0.
KOiK18384.
OMAiCPCGLVT.
OrthoDBiEOG75F4DB.
PhylomeDBiQ96EM0.
TreeFamiTF329167.

Miscellaneous databases

GenomeRNAii112849.
NextBioi78685.
PROiQ96EM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ96EM0.
CleanExiHS_C14orf149.
ExpressionAtlasiQ96EM0. baseline and differential.
GenevestigatoriQ96EM0.

Family and domain databases

InterProiIPR008794. Pro_racemase_fam.
[Graphical view]
PfamiPF05544. Pro_racemase. 1 hit.
[Graphical view]
PIRSFiPIRSF029792. Pro_racemase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  2. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Skin.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Identification of a human trans-3-Hydroxy-L-proline dehydratase, the first characterized member of a novel family of proline racemase-like enzymes."
    Visser W.F., Verhoeven-Duif N.M., de Koning T.J.
    J. Biol. Chem. 287:21654-21662(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, MUTAGENESIS OF THR-273.
  6. "Identification and characterization of trans-3-hydroxy-L-proline dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in trans-3-hydroxy-L-proline metabolism of bacteria."
    Watanabe S., Tanimoto Y., Yamauchi S., Tozawa Y., Sawayama S., Watanabe Y.
    FEBS Open Bio 4:240-250(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBUNIT.

Entry informationi

Entry nameiT3HPD_HUMAN
AccessioniPrimary (citable) accession number: Q96EM0
Secondary accession number(s): Q96LJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 18, 2010
Last modified: April 29, 2015
This is version 90 of the entry and version 2 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

Miscellaneous

In contrast to the T.cruzi proline racemase enzyme, lacks the conserved Cys at position 273 which is replaced by a Thr residue, transforming the racemase activity into dehydratase activity.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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.