Probable peptidylglycine alpha-hydroxylating monooxygenase
     (PHM)
     (EC 1.14.17.3)
Probable peptidyl-alpha-hydroxyglycine alpha-amidating lyase
     (EC 4.3.2.5)
     (Peptidylamidoglycolate lyase)
     (PAL)

Gene name

ORFNames:

T19B4.1

From

Caenorhabditis elegans

[TaxID: 6239]

Taxonomy

Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[2]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASS SPECTROMETRY. DOI=10.1038/nbt829; PubMed=12754521 [NCBI, ExPASy, EBI, Israel, Japan] Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.; "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."; Nat. Biotechnol. 21:667-672(2003).
[3]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M600392-MCP200; PubMed=17761667 [NCBI, ExPASy, EBI, Israel, Japan] Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.; "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."; Mol. Cell. Proteomics 6:2100-2109(2007).

Comments

FUNCTION: Probable bifunctional enzyme that catalyzes 2 sequencial steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O₂ = peptidyl(2-hydroxyglycine) + dehydroascorbate + H₂O.
CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide + glyoxylate.
COFACTOR: Zinc; for the lyase reaction (By similarity).
COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase reaction (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Secreted (Potential).
SIMILARITY: In the C-terminal section; belongs to the peptidyl-alpha-hydroxyglycine alpha-amidating lyase family.
SIMILARITY: In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family.
SIMILARITY: Contains 4 NHL repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U80438; AAB37637.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

T25895; T25895.

NP_491666.2; -.

3D structure databases

ModBase

P83388.

Organism-specific databases

WormBase

WBGene00020556; T19B4.1.

WormPep

T19B4.1; CE39282. [WormPep / WorfDB]

Family and domain databases

InterPro

IPR011042; 6-blade_b-propeller_TolB-like.
IPR014783; Cu2_ascorb_mOase_C.
IPR014784; Cu2_ascorb_mOase_like_C.
IPR000323; Cu2_ascorb_mOase_N.
IPR001258; NHL_repeat.
IPR013017; NHL_repeat_subgr.
IPR000720; Pep_amidat_mOase.
Graphical view of domain structure.

Gene3D

G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
G3DSA:2.60.120.230; Cu2_ascorb_mOase_core; 1.
G3DSA:2.60.120.310; Cu2_ascorb_mOase_core; 1.

Pfam

PF03712; Cu2_monoox_C; 1.
PF01082; Cu2_monooxygen; 1.
PF01436; NHL; 4.
Pfam graphical view of domain structure.

PRINTS

PR00790; PAMONOXGNASE.

PROSITE

PS00084; CU2_MONOOXYGENASE_1; FALSE_NEG.
PS00085; CU2_MONOOXYGENASE_2; 1.
PS51125; NHL; 3.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P83388.

Genome annotation databases

Ensembl

T19B4.1; Caenorhabditis elegans. [Contig view]

GeneID

266833; -.

KEGG

cel:T19B4.1; -.

Other

ProtoNet

P83388.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Copper; Glycoprotein; Lyase; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Repeat; Secreted; Signal; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`CHAIN`	`22 663`	`642`	`Probable peptidyl-glycine alpha-amidating monooxygenase T19B4.1.`	`PRO_0000248569`
`REPEAT`	`411 454`	`44`	`NHL 1.`
`REPEAT`	`464 507`	`44`	`NHL 2.`
`REPEAT`	`511 554`	`44`	`NHL 3.`
`REPEAT`	`626 656`	`31`	`NHL 4.`
`REGION`	`1 300`	`300`	`Peptidylglycine alpha-hydroxylating monooxygenase.`
`REGION`	`301 663`	`363`	`Peptidyl-alpha-hydroxyglycine alpha-amidating lyase.`
`METAL`	`75 75`		`Copper A (By similarity).`
`METAL`	`76 76`		`Copper A (By similarity).`
`METAL`	`142 142`		`Copper A (By similarity).`
`METAL`	`210 210`		`Copper B (By similarity).`
`METAL`	`212 212`		`Copper B (By similarity).`
`METAL`	`282 282`		`Copper B (By similarity).`
`CARBOHYD`	`191 191`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`269 269`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`411 411`		`N-linked (GlcNAc...).`
`DISULFID`	`82 98`		`By similarity.`
`DISULFID`	`194 305`		`By similarity.`
`DISULFID`	`261 283`		`By similarity.`
`DISULFID`	`478 497`		`By similarity.`

Sequence information

Length: 663 AA [This is the length of the unprocessed precursor]

Molecular weight: 74096 Da [This is the MW of the unprocessed precursor]

CRC64: 02D86AD68C1FFABE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNDRISINLI YLVLTFCCVS AATVRTAKND DIQKFTIQMI GYSPQKTDDY VAVSIEATPG 

        70         80         90        100        110        120 
YVVAFEPMAH ADRVHHMLLY GCTMPASEQG FWRGMETCGW GGGSYILYAW ARNAPNLVLP 

       130        140        150        160        170        180 
KDVAFSVGHE QDGIKYFVLQ VHYAQPFAGE VHDFSGVTMH ISQKKPMNLA AVMLFVSGTP 

       190        200        210        220        230        240 
IPPQLPAFQN NITCMFESST PIHPFAFRTH THAMGRLVSA FFKHDGHWTK IGKRNPQWPQ 

       250        260        270        280        290        300 
LFEGIPSKLM IGSGDQMSAS CRFDSMDKNR TVNMGAMGVD EMCNFYMMFH YDAKLDNPYP 

       310        320        330        340        350        360 
QGAICAKDYP SKMIDYPKDG FELLPSRPEL EHHAHQSKVP FGIVQEAIHE NLGGVKLGQV 

       370        380        390        400        410        420 
AGLAFNNEQQ LLVFQRAGRV WDASTFDNYN ILLDKKPIAD PVILVISYSG NQTKLERKLG 

       430        440        450        460        470        480 
GGQFYLPHGI YVDKDGFVYT TDVGSHTVAK WKIEGNELKN IWTSGELLMP GSDQHHYCKP 

       490        500        510        520        530        540 
TGITRVEDQL YVTDGYCNSR VVVLDLNGKR IRQFGLPGED AGQFNLPHDI VSDSAGRLLV 

       550        560        570        580        590        600 
TDRENGRVQH MTTQGHVIEE FKSTMFTNIY SAASHEDYVF MVPGRPIMGH ETEGIAVFVG 

       610        620        630        640        650        660 
RSGTGLIEYA FGPTTKGKRE QMGPQFGQPH CLRVCPDGGH IFVGDIAEGK ARLWQFKIRH 


DQN

P83388 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools