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Protein

Hyaluronate lyase

Gene

hylB

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

Functioni

Catalytic activityi

Cleaves hyaluronate chains at a beta-D-GlcNAc-(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)DescriptionActionsGraphical viewLength
Active sitei4291
Active sitei4791
Active sitei4881

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BRENDAi4.2.2.1. 5917.

Protein family/group databases

CAZyiCBM70. Carbohydrate-Binding Module Family 70.
PL8. 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
Proteomesi
  • UP000000823 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 40Sequence analysisAdd BLAST40
ChainiPRO_000002493241 – 984Hyaluronate lyaseAdd BLAST944

Proteomic databases

PRIDEiQ53591.

Interactioni

Protein-protein interaction databases

STRINGi211110.gbs1270.

Structurei

Secondary structure

1984
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi185 – 188Combined sources4
Beta strandi196 – 199Combined sources4
Beta strandi200 – 206Combined sources7
Helixi207 – 209Combined sources3
Beta strandi210 – 213Combined sources4
Beta strandi216 – 219Combined sources4
Beta strandi223 – 230Combined sources8
Beta strandi236 – 245Combined sources10
Helixi251 – 263Combined sources13
Helixi266 – 268Combined sources3
Helixi274 – 293Combined sources20
Helixi305 – 307Combined sources3
Helixi313 – 330Combined sources18
Turni336 – 339Combined sources4
Helixi341 – 357Combined sources17
Beta strandi367 – 369Combined sources3
Helixi371 – 375Combined sources5
Helixi377 – 388Combined sources12
Helixi390 – 392Combined sources3
Helixi395 – 408Combined sources14
Beta strandi414 – 416Combined sources3
Turni417 – 420Combined sources4
Helixi427 – 443Combined sources17
Helixi447 – 457Combined sources11
Helixi458 – 460Combined sources3
Beta strandi464 – 471Combined sources8
Beta strandi476 – 478Combined sources3
Turni479 – 481Combined sources3
Turni485 – 487Combined sources3
Helixi488 – 503Combined sources16
Helixi512 – 524Combined sources13
Helixi527 – 529Combined sources3
Helixi537 – 539Combined sources3
Helixi541 – 545Combined sources5
Helixi551 – 566Combined sources16
Helixi572 – 587Combined sources16
Beta strandi589 – 591Combined sources3
Helixi593 – 596Combined sources4
Helixi600 – 611Combined sources12
Beta strandi623 – 627Combined sources5
Helixi628 – 630Combined sources3
Beta strandi632 – 637Combined sources6
Turni638 – 641Combined sources4
Beta strandi642 – 647Combined sources6
Beta strandi653 – 655Combined sources3
Beta strandi660 – 662Combined sources3
Turni667 – 670Combined sources4
Beta strandi671 – 677Combined sources7
Turni681 – 684Combined sources4
Beta strandi685 – 687Combined sources3
Helixi688 – 691Combined sources4
Beta strandi694 – 696Combined sources3
Beta strandi701 – 703Combined sources3
Helixi712 – 716Combined sources5
Turni717 – 720Combined sources4
Helixi722 – 726Combined sources5
Beta strandi736 – 753Combined sources18
Beta strandi757 – 768Combined sources12
Beta strandi771 – 781Combined sources11
Beta strandi782 – 784Combined sources3
Beta strandi788 – 796Combined sources9
Beta strandi799 – 801Combined sources3
Beta strandi804 – 807Combined sources4
Beta strandi816 – 831Combined sources16
Beta strandi839 – 858Combined sources20
Helixi860 – 863Combined sources4
Beta strandi873 – 883Combined sources11
Beta strandi886 – 888Combined sources3
Beta strandi891 – 898Combined sources8
Helixi901 – 909Combined sources9
Beta strandi912 – 918Combined sources7
Beta strandi920 – 927Combined sources8
Turni928 – 931Combined sources4
Beta strandi932 – 937Combined sources6
Beta strandi943 – 945Combined sources3
Turni946 – 948Combined sources3
Beta strandi949 – 951Combined sources3
Beta strandi955 – 962Combined sources8
Beta strandi965 – 972Combined sources8
Turni973 – 976Combined sources4
Beta strandi977 – 981Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F1SX-ray2.10A171-984[»]
1I8QX-ray2.20A171-984[»]
1LXMX-ray2.20A171-984[»]
ProteinModelPortaliQ53591.
SMRiQ53591.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53591.

Family & Domainsi

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106AM8. Bacteria.
ENOG410XTFC. LUCA.
HOGENOMiHOG000008667.
KOiK01727.

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. GH-type_carb-bd.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45E → G in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti155 – 156SA → FV in AAA56749 (PubMed:7982914).Curated2
Sequence conflicti183E → K in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti246 – 251ASTEDK → GSPEDN in AAA56749 (PubMed:7982914).Curated6
Sequence conflicti267H → Y in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti279 – 280IN → LT in AAA56749 (PubMed:7982914).Curated2
Sequence conflicti288A → G in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti292 – 293KT → EA in AAA56749 (PubMed:7982914).Curated2
Sequence conflicti300H → R in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti384A → G in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti387A → S in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti413G → E in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti420D → V in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti583T → A in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti609M → L in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti639E → K in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti666D → G in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti676L → I in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti688 – 689FW → LG in AAA56749 (PubMed:7982914).Curated2
Sequence conflicti882Q → L in AAA56749 (PubMed:7982914).Curated1
Sequence conflicti894M → L in AAA56749 (PubMed:7982914).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15050 Genomic DNA. Translation: AAA56749.1.
AL766849 Genomic DNA. Translation: CAD46929.1. Different initiation.
PIRiA55137.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15050 Genomic DNA. Translation: AAA56749.1.
AL766849 Genomic DNA. Translation: CAD46929.1. Different initiation.
PIRiA55137.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F1SX-ray2.10A171-984[»]
1I8QX-ray2.20A171-984[»]
1LXMX-ray2.20A171-984[»]
ProteinModelPortaliQ53591.
SMRiQ53591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi211110.gbs1270.

Protein family/group databases

CAZyiCBM70. Carbohydrate-Binding Module Family 70.
PL8. Polysaccharide Lyase Family 8.

Proteomic databases

PRIDEiQ53591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4106AM8. Bacteria.
ENOG410XTFC. LUCA.
HOGENOMiHOG000008667.
KOiK01727.

Enzyme and pathway databases

BRENDAi4.2.2.1. 5917.

Miscellaneous databases

EvolutionaryTraceiQ53591.

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. GH-type_carb-bd.
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.
ProtoNetiSearch...

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: November 2, 2016
This is version 115 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.