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P43478

- CGKA_PSEVC

UniProt

P43478 - CGKA_PSEVC

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Protein
Kappa-carrageenase
Gene
cgkA
Organism
Pseudoalteromonas carrageenovora (Alteromonas carrageenovora)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in kappa-carrageenans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei163 – 1631Nucleophile
Active sitei165 – 1651
Active sitei168 – 1681Proton donor
Sitei260 – 2601Important for substrate recognition

GO - Molecular functioni

  1. kappa-carrageenase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16652.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Kappa-carrageenase (EC:3.2.1.83)
Gene namesi
Name:cgkA
OrganismiPseudoalteromonas carrageenovora (Alteromonas carrageenovora)
Taxonomic identifieri227 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 Publication
Add
BLAST
Chaini26 – 397372Kappa-carrageenase
PRO_0000011798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi98 ↔ 268

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 413
Helixi43 – 453
Turni54 – 563
Beta strandi57 – 604
Beta strandi67 – 693
Helixi71 – 733
Beta strandi74 – 774
Beta strandi80 – 9617
Helixi97 – 993
Beta strandi101 – 11212
Beta strandi114 – 1218
Beta strandi123 – 1319
Beta strandi137 – 14610
Beta strandi159 – 16810
Beta strandi172 – 1743
Beta strandi177 – 1793
Beta strandi182 – 1887
Beta strandi191 – 1955
Turni197 – 1993
Helixi201 – 2044
Beta strandi207 – 2093
Beta strandi219 – 2257
Beta strandi227 – 2348
Beta strandi237 – 2437
Beta strandi251 – 2599
Beta strandi263 – 2675
Beta strandi270 – 2734
Beta strandi283 – 29614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYPX-ray1.54A27-297[»]
ProteinModelPortaliP43478.
SMRiP43478. Positions 27-297.

Miscellaneous databases

EvolutionaryTraceiP43478.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR003343. Big_2.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
IPR008964. Invasin/intimin_cell_adhesion.
[Graphical view]
PfamiPF02368. Big_2. 1 hit.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
SMARTiSM00635. BID_2. 1 hit.
[Graphical view]
SUPFAMiSSF49373. SSF49373. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43478-1 [UniParc]FASTAAdd to Basket

« Hide

MKPISIVAFP IPAISMLLLS AVSQAASMQP PIAKPGETWI LQAKRSDEFN    50
VKDATKWNFQ TENYGVWSWK NENATVSNGK LKLTTKRESH QRTFWDGCNQ 100
QQVANYPLYY TSGVAKSRAT GNYGYYEARI KGASTFPGVS PAFWMYSTID 150
RSLTKEGDVQ YSEIDVVELT QKSAVRESDH DLHNIVVKNG KPTWMRPGSF 200
PQTNHNGYHL PFDPRNDFHT YGVNVTKDKI TWYVDGEIVG EKDNLYWHRQ 250
MNLTLSQGLR APHTQWKCNQ FYPSANKSAE GFPTSMEVDY VRTWVKVGNN 300
NSAPGEGQSC PNTFVAVNSV QLSAAKQTLR KGQSTTLEST VLPNCATNKK 350
VIYSSSNKNV ATVNSAGVVK AKNKGTATIT VKTKNKGKID KLTIAVN 397
Length:397
Mass (Da):44,224
Last modified:November 1, 1995 - v1
Checksum:iDA6D47C4682B10EF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71620 Genomic DNA. Translation: CAA50624.1.
PIRiI39507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X71620 Genomic DNA. Translation: CAA50624.1 .
PIRi I39507.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DYP X-ray 1.54 A 27-297 [» ]
ProteinModelPortali P43478.
SMRi P43478. Positions 27-297.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16652.

Miscellaneous databases

EvolutionaryTracei P43478.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR003343. Big_2.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
IPR008964. Invasin/intimin_cell_adhesion.
[Graphical view ]
Pfami PF02368. Big_2. 1 hit.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view ]
SMARTi SM00635. BID_2. 1 hit.
[Graphical view ]
SUPFAMi SSF49373. SSF49373. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEi PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The gene encoding the kappa-carrageenase of Alteromonas carrageenovora is related to beta-1,3-1,4-glucanases."
    Barbeyron T., Henrissat B., Kloareg B.
    Gene 139:105-109(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-30 AND 33-37.
    Strain: ATCC 43555 / DSM 6820 / IAM 12662 / NBRC 12985 / NCIMB 302.
  2. "The kappa-carrageenase of P. carrageenovora features a tunnel-shaped active site: a novel insight in the evolution of Clan-B glycoside hydrolases."
    Michel G., Chantalat L., Duee E., Barbeyron T., Henrissat B., Kloareg B., Dideberg O.
    Structure 9:513-525(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 27-297.

Entry informationi

Entry nameiCGKA_PSEVC
AccessioniPrimary (citable) accession number: P43478
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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