Peptidylglycine alpha-hydroxylating monooxygenase B
     (PHM-B)
     (EC 1.14.17.3)
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase B
     (EC 4.3.2.5)
     (Peptidylamidoglycolate lyase-B)
     (PAL-B)

Gene name

Name:

pam-B

From

Xenopus laevis (African clawed frog)

[TaxID: 8355]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skin;
DOI=10.1016/0006-291X(88)90767-X; PubMed=2829895 [NCBI, ExPASy, EBI, Israel, Japan]
Ohsuye K., Kitano K., Wada Y., Fuchimura K., Tanaka S., Mizuno K., Matsuo H.;
"Cloning of cDNA encoding a new peptide C-terminal alpha-amidating enzyme having a putative membrane-spanning domain from Xenopus laevis skin.";
Biochem. Biophys. Res. Commun. 150:1275-1281(1988).

Comments

FUNCTION: 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 (By similarity).
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: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein (By similarity). Note=Secretory granules.
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

M19032; AAA49667.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A27715; URXLA2.

NP_001081254.1; -.

3D structure databases

HSSP

P14925; 1PHM. [HSSP ENTRY / PDB]

ModBase

P12890.

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; 1.
PS00085; CU2_MONOOXYGENASE_2; 1.
PS51125; NHL; 4.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P12890.

Genome annotation databases

GeneID

397736; -.

KEGG

xla:397736; -.

Phylogenomic databases

HOVERGEN

P12890; -.

Other

ProtoNet

P12890.

UniRef

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

Keywords

Copper; Cytoplasmic vesicle; Glycoprotein; Lyase; Membrane; Metal-binding; Monooxygenase; Multifunctional enzyme; Oxidoreductase; Repeat; Signal; Transmembrane; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 39`	`39`	`Potential.`
`CHAIN`	`40 875`	`836`	`Peptidyl-glycine alpha-amidating monooxygenase B.`	`PRO_0000006368`
`TOPO_DOM`	`40 763`	`724`	`Intragranular (Potential).`
`TRANSMEM`	`764 787`	`24`	`Potential.`
`TOPO_DOM`	`788 875`	`88`	`Cytoplasmic (Potential).`
`REPEAT`	`467 508`	`42`	`NHL 1.`
`REPEAT`	`516 561`	`46`	`NHL 2.`
`REPEAT`	`569 613`	`45`	`NHL 3.`
`REPEAT`	`666 709`	`44`	`NHL 4.`
`REGION`	`3 394`	`392`	`Peptidylglycine alpha-hydroxylating monooxygenase (By similarity).`
`REGION`	`395 716`	`322`	`Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (By similarity).`
`METAL`	`105 105`		`Copper A (By similarity).`
`METAL`	`106 106`		`Copper A (By similarity).`
`METAL`	`170 170`		`Copper A (By similarity).`
`METAL`	`240 240`		`Copper B (By similarity).`
`METAL`	`242 242`		`Copper B (By similarity).`
`METAL`	`312 312`		`Copper B (By similarity).`
`CARBOHYD`	`465 465`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`662 662`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`743 743`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`45 184`		`By similarity.`
`DISULFID`	`79 124`		`By similarity.`
`DISULFID`	`112 129`		`By similarity.`
`DISULFID`	`225 332`		`By similarity.`
`DISULFID`	`291 313`		`By similarity.`
`DISULFID`	`530 551`		`By similarity.`
`DISULFID`	`598 609`		`By similarity.`

Sequence information

Length: 875 AA [This is the length of the unprocessed precursor]

Molecular weight: 97085 Da [This is the MW of the unprocessed precursor]

CRC64: C07373AF6BF13450 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDMASLISSL LVLFLIFQNS CYCFRSPLSV FKRYEESTRS LSNDCLGTTR PVMSPGSSDY 

        70         80         90        100        110        120 
TLDIRMPGVT PTESDTYLCK SYRLPVDDEA YVVDYRPHAN MDTAHHMLLF GCNVPSSTDD 

       130        140        150        160        170        180 
YWDCSAGTCN DKSSIMYAWA KNAPPTKLPE GVGFQVGGKS GSRYFVLQVH YGDVKAFQDK 

       190        200        210        220        230        240 
HKDCTGVTVR ITPEKQPLIA GIYLSMSLNT VVPPGQEVVN SDIACLYNRP TIHPFAYRVH 

       250        260        270        280        290        300 
THQLGQVVSG FRVRHGKWTL IGRQSPQLPQ AFYPVEHPLE ISPGDIIATR CLFTGKGRMS 

       310        320        330        340        350        360 
ATYIGGTAKD EMCNLYIMYY MDAAHATSYM TCVQTGNPKL FENIPEIANV PIPVSPDMMM 

       370        380        390        400        410        420 
MMMMGHGHHH TEAEAETNTA LQQPKREEEE VLNQDVHLEE DTDWPGVNLK VGQVSGLALD 

       430        440        450        460        470        480 
PKNNLVIFHR GDHVWDENSF DRNFVYQQRG IGPIQESTIL VVDPNTSKVL KSTGQNLFFL 

       490        500        510        520        530        540 
PHGLTIDRDG NYWVTDVALH QVFKVGAEKE TPLLVLGRAF QPGSDRKHFC QPTDVAVDPI 

       550        560        570        580        590        600 
TGNFFVADGY CNSRIMQFSP NGMFIMQWGE ETSSNLPRPG QFRIPHSLTM ISDQGQLCVA 

       610        620        630        640        650        660 
DRENGRIQCF HAKTGEFVKQ IKHQEFGREV FAVSYAPGGV LYAVNGKPYY GDSTPVQGFM 

       670        680        690        700        710        720 
LNFSNGDILD TFIPARKNFE MPHDIAAGDD GTVYVGDAHA NAVWKFSPSK AEHRSVKKAG 

       730        740        750        760        770        780 
IEVEEITETE IFETHMRSRP KTNESVGQQT QEKPSVVQES SAGVSFVLII TLLIIPVVVL 

       790        800        810        820        830        840 
IAIAIFIRWR KVRMYGGDIG HKSESSSGGI LGKLRGKGSG GLNLGTFFAT HKGYSRKGFD 

       850        860        870 
RLSTEGSDQE KDDDDDGSDS EEEYSAPPIP PVSSS

P12890 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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