Heparinase II protein precursor - Pedobacter heparinus

Preferred order of sections

Names and origin

Protein names

Submitted name:
Heparinase II protein EMBL AAB18277.1

Gene names

Name:

HepB EMBL AAB18277.1

Organism

Pedobacter heparinus (Flavobacterium heparinum) EMBL AAB18277.1

Taxonomic identifier

984 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Sphingobacteriia › Sphingobacteriales › Sphingobacteriaceae › Pedobacter

Protein attributes

Sequence length	772 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Signal EMBL AAB18277.1
Ligand	Metal-binding PDB 3E7J PDB 2FUQ PDB 3E80 PDB 2FUT Zinc PDB 3E7J PDB 2FUQ PDB 3E80 PDB 2FUT
Technical term	3D-structure PDB 3E7J PDB 2FUQ PDB 3E80 PDB 2FUT
Gene Ontology (GO)
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential EMBL AAB18277.1

Chain

26 – 772

747

Potential EMBL AAB18277.1

PRO_5000144613

Regions

Region

436 – 437

2

N-acetyl-D-glucosamine binding PDB 3E7J

Sites

Metal binding

408

1

Zinc; via pros nitrogen PDB 3E7J PDB 2FUQ PDB 3E80 PDB 2FUT

Metal binding

425

1

Zinc PDB 3E7J PDB 2FUQ PDB 3E80 PDB 2FUT

Metal binding

451

1

Zinc; via tele nitrogen PDB 3E7J PDB 2FUQ PDB 3E80 PDB 2FUT

Binding site

96

1

N-acetyl-D-glucosamine PDB 3E7J

Binding site

148

1

N-acetyl-D-glucosamine PDB 3E7J

Binding site

405

1

N-acetyl-D-glucosamine PDB 3E7J

Binding site

470

1

N-acetyl-D-glucosamine; via amide nitrogen PDB 3E7J

Amino acid modifications

Glycosylation

134

1

O-linked (Man...) PDB 2FUQ PDB 3E80

Sequences

Sequence

Length

Mass (Da)

Tools

Q46080 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 66D9752035420E8C
Show »

FASTA

772

87,652

        10         20         30         40         50         60 
MKRQLYLYVI FVVVELMVFT TKGYSQTKAD VVWKDVDGVS MPIPPKTHPR LYLREQQVPD 

        70         80         90        100        110        120 
LKNRMNDPKL KKVWADMIKM QEDWKPADIP EVKDFRFYFN QKGLTVRVEL MALNYLMTKD 

       130        140        150        160        170        180 
PKVGREAITS IIDTLETATF KPAGDISRGI GLFMVTGAIV YDWCYDQLKP EEKTRFVKAF 

       190        200        210        220        230        240 
VRLAKMLECG YPPVKDKSIV GHASEWMIMR DLLSVGIAIY DEFPEMYNLA AGRFFKEHLV 

       250        260        270        280        290        300 
ARNWFYPSHN YHQGMSYLNV RFTNDLFALW ILDRMGAGNV FNPGQQFILY DAIYKRRPDG 

       310        320        330        340        350        360 
QILAGGDVDY SRKKPKYYTM PALLAGSYYK DEYLNYEFLK DPNVEPHCKL FEFLWRDTQL 

       370        380        390        400        410        420 
GSRKPDDLPL SRYSGSPFGW MIARTGWGPE SVIAEMKVNE YSFLNHQHQD AGAFQIYYKG 

       430        440        450        460        470        480 
PLAIDAGSYT GSSGGYNSPH NKNFFKRTIA HNSLLIYDPK ETFSSSGYGG SDHTDFAAND 

       490        500        510        520        530        540 
GGQRLPGKGW IAPRDLKEML AGDFRTGKIL AQGFGPDNQT PDYTYLKGDI TAAYSAKVKE 

       550        560        570        580        590        600 
VKRSFLFLNL KDAKVPAAMI VFDKVVASNP DFKKFWLLHS IEQPEIKGNQ ITIKRTKNGD 

       610        620        630        640        650        660 
SGMLVNTALL PDAANSNITS IGGKGKDFWV FGTNYTNDPK PGTDEALERG EWRVEITPKK 

       670        680        690        700        710        720 
AAAEDYYLNV IQIADNTQQK LHEVKRIDGD KVVGVQLADR IVTFSKTSET VDRPFGFSVV 

       730        740        750        760        770 
GKGTFKFVMT DLLPGTWQVL KDGKILYPAL SAKGDDGPLY FEGTEGTYRF LR

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References

[1]	"Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum." Su H., Blain F., Musil R.A., Zimmermann J.J., Gu K., Bennett D.C. Appl. Environ. Microbiol. 62:2723-2734(1996) [PubMed: 8702264] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Tkalec A.L. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Crystal structure of heparinase II from Pedobacter heparinus and its complex with a disaccharide product." Shaya D., Tocilj A., Li Y., Myette J., Venkataraman G., Sasisekharan R., Cygler M. J. Biol. Chem. 281:15525-15535(2006) [PubMed: 16565082] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 27-772 IN COMPLEX WITH ZINC, GLYCOSYLATION AT THR-134.
[4]	"Catalytic mechanism of heparinase II investigated by site-directed mutagenesis and the crystal structure with its substrate." Shaya D., Zhao W., Garron M.L., Xiao Z., Cui Q., Zhang Z., Sulea T., Linhardt R.J., Cygler M. J. Biol. Chem. 285:20051-20061(2010) [PubMed: 20404324] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 24-772 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE AND ZINC, GLYCOSYLATION AT THR-134.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U27585 Genomic DNA. Translation: AAB18277.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2FUQ	X-ray	2.15	A/B	27-772	[»]
2FUT	X-ray	2.30	A/B	25-772	[»]
3E7J	X-ray	2.10	A/B	24-772	[»]
3E80	X-ray	2.35	A/B/C	24-772	[»]

ProteinModelPortal

Q46080.

SMR

Q46080. Positions 30-772.

ModBase

Search...

Protein family/group databases

CAZy

PL21. Polysaccharide Lyase Family 21.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008929. Chondroitin_lyas.
IPR012480. Hepar_II_III.
[Graphical view]

Pfam

PF07940. Hepar_II_III. 1 hit.
[Graphical view]

SUPFAM

SSF48230. Chondroitin_lyas. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q46080_PEDHE

Accession

Primary (citable) accession number: Q46080

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)