Reviewed, UniProtKB/Swiss-Prot Q05819 (HEP1_PEDHE)

Names and origin

Protein names	Recommended name:     Heparin lyase I       Short name=Heparinase I     EC=4.2.2.7
Organism	Pedobacter heparinus (Flavobacterium heparinum)
Taxonomic identifier	984 [NCBI]
Taxonomic lineage	Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Sphingobacteriaceae › Pedobacter

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Degrades heparin and heparan sulfate. Also implicated in the release of heparin-bound growth factors from the extracellular matrix.
Catalytic activity	Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends.
Subunit structure	Monomer.
Subcellular location	Periplasm.
Induction	By heparin.
Post-translational modification	The N-terminus is blocked.
biophysicochemical properties	Kinetic parameters: KM=33 µM for native heparinase KM=47 µM for recombinant heparinase
Mass spectrometry	Molecular mass is 42502±2.8 Da from positions 22 - 384. Determined by ESI. Ref.3

Ontologies

Keywords
Cellular component	Periplasm
Domain	Signal
Ligand	Heparin-binding
Molecular function	Lyase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW heparin lyase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Ref.2
	Chain	22 – 384	363	Heparin lyase I		PRO_0000021411
Amino acid modifications
	Modified residue	22	1	Blocked amino end (Gln)
	Glycosylation	39	1	O-linked (Man...) Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q05819-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: B082E0B571DEA699	FASTA	384	43,807
	10 20 30 40 50 60 MKKQILYLIV LQQLFLCSAY AQQKKSGNIP YRVNVQADSA KQKAIIDNKW VAVGINKPYA 70 80 90 100 110 120 LQYDDKLRFN GKPSYRFELK AEDNSLEGYA AGETKGRTEL SYSYATTNDF KKFPPSVYQN 130 140 150 160 170 180 AQKLKTVYHY GKGICEQGSS RSYTFSVYIP SSFPDNATTI FAQWHGAPSR TLVATPEGEI 190 200 210 220 230 240 KTLSIEEFLA LYDRMIFKKN IAHDKVEKKD KDGKITYVAG KPNGWKVEQG GYPTLAFGFS 250 260 270 280 290 300 KGYFYIKANS DRQWLTDKAD RNNANPENSE VMKPYSSEYK TSTIAYKMPF AQFPKDCWIT 310 320 330 340 350 360 FDVAIDWTKY GKEANTILKP GKLDVMMTYT KNKKPQKAHI VNQQEILIGR NDDDGYYFKF 370 380 GIYRVGNSTV PVTYNLSGYS ETAR

References

[1]	"Cloning and expression of heparinase I gene from Flavobacterium heparinum." Sasisekharan R., Bulmer M., Moremen K.W., Cooney C.L., Langer R. Proc. Natl. Acad. Sci. U.S.A. 90:3660-3664(1993) [PubMed: 8475114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum." Ernst S., Venkataraman G., Winkler S., Godavarti R., Langer R., Cooney C.L., Sasisekharan R. Biochem. J. 315:589-597(1996) [PubMed: 8615834] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-27, CHARACTERIZATION.
[3]	"Structural characterization of the novel O-linked carbohydrate structure of Flavobacterium heparinum heparinase I." Huang L., van Halbeek H., Eggimann B., Zimmermannn J. Glycobiology 5:712-712(1995) Cited for: GLYCOSYLATION AT SER-39, STRUCTURE OF CARBOHYDRATE, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L12534 Genomic DNA. Translation: AAA24920.1.
PIR	A47479.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	PL13. Polysaccharide Lyase Family 13.
Enzyme and pathway databases
BRENDA	4.2.2.7. 279142.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

HEP1_PEDHE

Accession

Primary (citable) accession number: Q05819

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)