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Q00757 (CHSB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chitin synthase B
EC=2.4.1.16
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase B
Class-III chitin synthase B
Gene names
Name:chsB
ORF Names:AN2523
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a major role in cell wall biogenesis.

Catalytic activity

UDP-N-acetyl-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1).

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the chitin synthase family. Class III subfamily.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

chitin biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionchitin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916Chitin synthase B
PRO_0000193692

Regions

Transmembrane544 – 56118Helical; Potential
Transmembrane588 – 60821Helical; Potential
Transmembrane629 – 64921Helical; Potential
Transmembrane664 – 68421Helical; Potential
Transmembrane716 – 73621Helical; Potential
Transmembrane845 – 86521Helical; Potential
Transmembrane884 – 90421Helical; Potential

Experimental info

Sequence conflict136 – 1372AG → RR in BAA04807. Ref.1
Sequence conflict136 – 1372AG → RR in BAA11845. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q00757 [UniParc].

Last modified May 26, 2009. Version 2.
Checksum: 622356DC99AA4B5E

FASTA916101,882
        10         20         30         40         50         60 
MAYHGSGPQS PGEHTYDDGH QLRDLSHSNT SYEEEASHGL LSSQQSPFAG PFDDPHQQRG 

        70         80         90        100        110        120 
LTASPVQRPT SGYSLTESYA PDAAYHDPYS ANQSVYSGHS ENPAAAFGVP GRVASPYARS 

       130        140        150        160        170        180 
ETSSTEAWRQ RQAGAAGGGN GLRRYATRKV KLVQGSVLSV DYPVPSAIQN AIQAKYRNDL 

       190        200        210        220        230        240 
EGGSEEFTHM RYTAATCDPN EFTLHNGYNL RPAMYNRHTE LLIAITYYNE DKTLTARTLH 

       250        260        270        280        290        300 
GVMQNIRDIV NLKKSEFWNK GGPAWQKIVV CLVFDGIDPC DKDTLDVLAT VGIYQDGVMK 

       310        320        330        340        350        360 
RDVDGKETVA HIFEYTTQLS VTPNQQLIRP TDDGPSTLPP VQMMFCLKQK NSKKINSHRW 

       370        380        390        400        410        420 
LFNAFGRILN PEVCILLDAG TKPGPKSLLY LWEAFYNDKD LGGACGEIHA MLGKGWKKLL 

       430        440        450        460        470        480 
NPLVAAQNFE YKISNILDKP LESSFGYVSV LPGAFSAYRF RAIMGRPLEQ YFHGDHTLSK 

       490        500        510        520        530        540 
QLGKKGIEGM NIFKKNMFLA EDRILCFELV AKAGSKWHLS YVKASKGETD VPEGAPEFIS 

       550        560        570        580        590        600 
QRRRWLNGSF AAGIYSLMHF GRMYKSGHNI VRMFFLHLQM LYNWFSTFLT WFSLASYWLT 

       610        620        630        640        650        660 
TSVIMDLVGT PSSSNGYTAF PFGKTATPII NTLVKYIYLA FLLLQFILAL GNRPKGSKLS 

       670        680        690        700        710        720 
YLASFVAFGI IQLYVVVDAL YLVVRAFTGG APMDFNTDDG IGAFLSSFFG SSGAGIIIIA 

       730        740        750        760        770        780 
LAATFGLYFV ASFMYLDPWH MFTSFPAYMA VQSSYINILN VYAFSNWHDV SWGTKGSDKA 

       790        800        810        820        830        840 
DALPSAKTTG GKGEEAVIEE IDKPQADIDS QFEATVKRAL TPYVPPEEKE EKSLDDSYKS 

       850        860        870        880        890        900 
FRTRLVTLWL FSNGLLAVCI TSEGLDKFGF TNTSTERTSR FFQALLWSNA VVALIRFIGA 

       910 
TWFLGKTGLL CCFARR

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of two chitin synthase genes from Aspergillus nidulans."
Yanai K., Kojima N., Takaya N., Horiuchi H., Ohta A., Takagi M.
Biosci. Biotechnol. Biochem. 58:1828-1835(1994) [PubMed: 7765508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FGSC 89.
[2]"Aspergillus nidulans chitin synthase B gene."
Tatsuno K.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FGSC 89.
[3]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[4]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D21269 Genomic DNA. Translation: BAA04807.1.
D83216 mRNA. Translation: BAA11845.1.
AACD01000043 Genomic DNA. Translation: EAA64628.1.
BN001307 Genomic DNA. Translation: CBF87020.1.
PIRJC2315.
RefSeqXP_660127.1. XM_655035.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00009248; CADANIAP00009248; CADANIAG00009248.
GeneID2874737.
KEGGani:AN2523.2.

Phylogenomic databases

OMAMHFGRMY.
OrthoDBEOG405W8B.
PhylomeDBQ00757.

Enzyme and pathway databases

BRENDA2.4.1.16. 517.

Family and domain databases

InterProIPR004834. Chitin_synth.
IPR013616. Chitin_synth_N.
[Graphical view]
KOK00698.
PfamPF01644. Chitin_synth_1. 1 hit.
PF08407. Chitin_synth_1N. 1 hit.
[Graphical view]
ProDomPD002998. Chitin_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameCHSB_EMENI
AccessionPrimary (citable) accession number: Q00757
Secondary accession number(s): C8VPK2, P87326, Q5BAA7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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