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Q53591

- HYSA_STRA3

UniProt

Q53591 - HYSA_STRA3

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Protein

Hyaluronate lyase

Gene

hylB

Organism
Streptococcus agalactiae serotype III (strain NEM316)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei429 – 4291
Active sitei479 – 4791
Active sitei488 – 4881

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. hyaluronate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BRENDAi4.2.2.1. 5917.

Protein family/group databases

CAZyiPL8. Polysaccharide Lyase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronate lyase (EC:4.2.2.1)
Alternative name(s):
Hyaluronidase
Short name:
HYase
Gene namesi
Name:hylB
Ordered Locus Names:gbs1270
OrganismiStreptococcus agalactiae serotype III (strain NEM316)
Taxonomic identifieri211110 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000823: Chromosome

Organism-specific databases

GenoListigbs1270.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040Sequence AnalysisAdd
BLAST
Chaini41 – 984944Hyaluronate lyasePRO_0000024932Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi211110.gbs1270.

Structurei

Secondary structure

1
984
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi185 – 1884
Beta strandi196 – 1994
Beta strandi200 – 2067
Helixi207 – 2093
Beta strandi210 – 2134
Beta strandi216 – 2194
Beta strandi223 – 2308
Beta strandi236 – 24510
Helixi251 – 26313
Helixi266 – 2683
Helixi274 – 29320
Helixi305 – 3073
Helixi313 – 33018
Turni336 – 3394
Helixi341 – 35717
Beta strandi367 – 3693
Helixi371 – 3755
Helixi377 – 38812
Helixi390 – 3923
Helixi395 – 40814
Beta strandi414 – 4163
Turni417 – 4204
Helixi427 – 44317
Helixi447 – 45711
Helixi458 – 4603
Beta strandi464 – 4718
Beta strandi476 – 4783
Turni479 – 4813
Turni485 – 4873
Helixi488 – 50316
Helixi512 – 52413
Helixi527 – 5293
Helixi537 – 5393
Helixi541 – 5455
Helixi551 – 56616
Helixi572 – 58716
Beta strandi589 – 5913
Helixi593 – 5964
Helixi600 – 61112
Beta strandi623 – 6275
Helixi628 – 6303
Beta strandi632 – 6376
Turni638 – 6414
Beta strandi642 – 6476
Beta strandi653 – 6553
Beta strandi660 – 6623
Turni667 – 6704
Beta strandi671 – 6777
Turni681 – 6844
Beta strandi685 – 6873
Helixi688 – 6914
Beta strandi694 – 6963
Beta strandi701 – 7033
Helixi712 – 7165
Turni717 – 7204
Helixi722 – 7265
Beta strandi736 – 75318
Beta strandi757 – 76812
Beta strandi771 – 78111
Beta strandi782 – 7843
Beta strandi788 – 7969
Beta strandi799 – 8013
Beta strandi804 – 8074
Beta strandi816 – 83116
Beta strandi839 – 85820
Helixi860 – 8634
Beta strandi873 – 88311
Beta strandi886 – 8883
Beta strandi891 – 8988
Helixi901 – 9099
Beta strandi912 – 9187
Beta strandi920 – 9278
Turni928 – 9314
Beta strandi932 – 9376
Beta strandi943 – 9453
Turni946 – 9483
Beta strandi949 – 9513
Beta strandi955 – 9628
Beta strandi965 – 9728
Turni973 – 9764
Beta strandi977 – 9815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1SX-ray2.10A171-984[»]
1I8QX-ray2.20A171-984[»]
1LXMX-ray2.20A171-984[»]
ProteinModelPortaliQ53591.
SMRiQ53591. Positions 171-984.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53591.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG305085.
HOGENOMiHOG000008667.
KOiK01727.
OrthoDBiEOG6GBM67.

Family and domain databases

Gene3Di1.50.10.100. 1 hit.
2.60.220.10. 1 hit.
2.60.40.1380. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR008929. Chondroitin_lyas.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR023295. Hyaluronate_lyase_beta_dom.
IPR014756. Ig_E-set.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view]
PfamiPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q53591-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKQVVDNQTQ NKELVKNGDF NQTNPVSGSW SHTSAREWSA WIDKENTADK
60 70 80 90 100
SPIIQRTEQG QVSLSSDKGF RGAVTQKVNI DPTKKYEVKF DIETSNKAGQ
110 120 130 140 150
AFLRIMEKKD NNTRLWLSEM TSGTTNKHTL TKIYNPKLNV SEVTLELYYE
160 170 180 190 200
KGTGSATFDN ISMKAKGPKD SEHPQPVTTQ IEESVNTALN KNYVFNKADY
210 220 230 240 250
QYTLTNPSLG KIVGGILYPN ATGSTTVKIS DKSGKIIKEV PLSVTASTED
260 270 280 290 300
KFTKLLDKWN DVTIGNHVYD TNDSNMQKIN QKLDETNAKN IKTIKLDSNH
310 320 330 340 350
TFLWKDLDNL NNSAQLTATY RRLEDLAKQI TNPHSTIYKN EKAIRTVKES
360 370 380 390 400
LAWLHQNFYN VNKDIEGSAN WWDFEIGVPR SITATLALMN NYFTDAEIKT
410 420 430 440 450
YTDPIEHFVP DAGYFRKTLD NPFKALGGNL VDMGRVKIIE GLLRKDNTII
460 470 480 490 500
EKTSHSLKNL FTTATKAEGF YADGSYIDHT NVAYTGAYGN VLIDGLTQLL
510 520 530 540 550
PIIQETDYKI SNQELDMVYK WINQSFLPLI VKGELMDMSR GRSISREAAS
560 570 580 590 600
SHAAAVEVLR GFLRLANMSN EERNLDLKST IKTIITSNKF YNVFNNLKSY
610 620 630 640 650
SDIANMNKML NDSTVATKPL KSNLSTFNSM DRLAYYNAEK DFGFALSLHS
660 670 680 690 700
KRTLNYEGMN DENTRDWYTG DGMFYLYNSD QSHYSNHFWP TVNPYKMAGT
710 720 730 740 750
TEKDAKREDT TKEFMSKHSK DAKEKTGQVT GTSDFVGSVK LNDHFALAAM
760 770 780 790 800
DFTNWDRTLT AQKGWVILND KIVFLGSNIK NTNGIGNVST TIDQRKDDSK
810 820 830 840 850
TPYTTYVNGK TIDLKQASSQ QFTDTKSVFL ESKEPGRNIG YIFFKNSTID
860 870 880 890 900
IERKEQTGTW NSINRTSKNT SIVSNPFITI SQKHDNKGDS YGYMMVPNID
910 920 930 940 950
RTSFDKLANS KEVELLENSS KQQVIYDKNS QTWAVIKHDN QESLINNQFK
960 970 980
MNKAGLYLVQ KVGNDYQNVY YQPQTMTKTD QLAI
Length:984
Mass (Da):111,581
Last modified:January 17, 2003 - v2
Checksum:iAC7215ED6D5C2592
GO

Sequence cautioni

The sequence CAD46929.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451E → G in AAA56749. (PubMed:7982914)Curated
Sequence conflicti155 – 1562SA → FV in AAA56749. (PubMed:7982914)Curated
Sequence conflicti183 – 1831E → K in AAA56749. (PubMed:7982914)Curated
Sequence conflicti246 – 2516ASTEDK → GSPEDN in AAA56749. (PubMed:7982914)Curated
Sequence conflicti267 – 2671H → Y in AAA56749. (PubMed:7982914)Curated
Sequence conflicti279 – 2802IN → LT in AAA56749. (PubMed:7982914)Curated
Sequence conflicti288 – 2881A → G in AAA56749. (PubMed:7982914)Curated
Sequence conflicti292 – 2932KT → EA in AAA56749. (PubMed:7982914)Curated
Sequence conflicti300 – 3001H → R in AAA56749. (PubMed:7982914)Curated
Sequence conflicti384 – 3841A → G in AAA56749. (PubMed:7982914)Curated
Sequence conflicti387 – 3871A → S in AAA56749. (PubMed:7982914)Curated
Sequence conflicti413 – 4131G → E in AAA56749. (PubMed:7982914)Curated
Sequence conflicti420 – 4201D → V in AAA56749. (PubMed:7982914)Curated
Sequence conflicti583 – 5831T → A in AAA56749. (PubMed:7982914)Curated
Sequence conflicti609 – 6091M → L in AAA56749. (PubMed:7982914)Curated
Sequence conflicti639 – 6391E → K in AAA56749. (PubMed:7982914)Curated
Sequence conflicti666 – 6661D → G in AAA56749. (PubMed:7982914)Curated
Sequence conflicti676 – 6761L → I in AAA56749. (PubMed:7982914)Curated
Sequence conflicti688 – 6892FW → LG in AAA56749. (PubMed:7982914)Curated
Sequence conflicti882 – 8821Q → L in AAA56749. (PubMed:7982914)Curated
Sequence conflicti894 – 8941M → L in AAA56749. (PubMed:7982914)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U15050 Genomic DNA. Translation: AAA56749.1.
AL766849 Genomic DNA. Translation: CAD46929.1. Different initiation.
PIRiA55137.
RefSeqiNP_735714.1. NC_004368.1.

Genome annotation databases

EnsemblBacteriaiCAD46929; CAD46929; CAD46929.
GeneIDi1030294.
KEGGisan:gbs1270.
PATRICi19638423. VBIStrAga3577_1300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U15050 Genomic DNA. Translation: AAA56749.1 .
AL766849 Genomic DNA. Translation: CAD46929.1 . Different initiation.
PIRi A55137.
RefSeqi NP_735714.1. NC_004368.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F1S X-ray 2.10 A 171-984 [» ]
1I8Q X-ray 2.20 A 171-984 [» ]
1LXM X-ray 2.20 A 171-984 [» ]
ProteinModelPortali Q53591.
SMRi Q53591. Positions 171-984.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 211110.gbs1270.

Protein family/group databases

CAZyi PL8. Polysaccharide Lyase Family 8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD46929 ; CAD46929 ; CAD46929 .
GeneIDi 1030294.
KEGGi san:gbs1270.
PATRICi 19638423. VBIStrAga3577_1300.

Organism-specific databases

GenoListi gbs1270.

Phylogenomic databases

eggNOGi NOG305085.
HOGENOMi HOG000008667.
KOi K01727.
OrthoDBi EOG6GBM67.

Enzyme and pathway databases

BRENDAi 4.2.2.1. 5917.

Miscellaneous databases

EvolutionaryTracei Q53591.

Family and domain databases

Gene3Di 1.50.10.100. 1 hit.
2.60.220.10. 1 hit.
2.60.40.1380. 1 hit.
2.70.98.10. 1 hit.
InterProi IPR008929. Chondroitin_lyas.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR023295. Hyaluronate_lyase_beta_dom.
IPR014756. Ig_E-set.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view ]
Pfami PF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48230. SSF48230. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of the gene for group B streptococcal hyaluronate lyase."
    Lin B., Hollingshead S.K., Coligan J.E., Egan M.L., Baker J.R., Pritchard D.G.
    J. Biol. Chem. 269:30113-30116(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 3502 / Serotype III.
  2. "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease."
    Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.
    Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NEM316.
  3. "Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate lyase."
    Li S., Jedrzejas M.J.
    J. Biol. Chem. 276:41407-41416(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 171-984.

Entry informationi

Entry nameiHYSA_STRA3
AccessioniPrimary (citable) accession number: Q53591
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 17, 2003
Last modified: October 29, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3