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C3NGY2 (C3NGY2_SULIN) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine By similarity. HAMAP-Rule MF_01024 PIRNR PIRNR000099

Catalytic activity

L-histidinol + H2O + 2 NAD+ = L-histidine + 2 NADH. HAMAP-Rule MF_01024 PIRNR PIRNR000099

Cofactor

Binds 1 zinc ion per subunit By similarity. PIRSR PIRSR000099-4 HAMAP-Rule MF_01024

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. HAMAP-Rule MF_01024 PIRNR PIRNR000099

Sequence similarities

Belongs to the histidinol dehydrogenase family. HAMAP-Rule MF_01024 PIRNR PIRNR000099 RuleBase RU004175

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site2981Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024
Active site2991Proton acceptor By similarity PIRSR PIRSR000099-1 HAMAP-Rule MF_01024
Metal binding2441Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding2471Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding3311Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Metal binding3891Zinc By similarity PIRSR PIRSR000099-4 HAMAP-Rule MF_01024
Binding site1141NAD By similarity HAMAP-Rule MF_01024 PIRSR PIRSR000099-2
Binding site1761NAD By similarity HAMAP-Rule MF_01024 PIRSR PIRSR000099-2
Binding site1991NAD By similarity HAMAP-Rule MF_01024 PIRSR PIRSR000099-2
Binding site2221Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2441Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2471Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site2991Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3311Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3841Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024
Binding site3891Substrate By similarity PIRSR PIRSR000099-3 HAMAP-Rule MF_01024

Sequences

Sequence LengthMass (Da)Tools
C3NGY2 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 5642CBB806FA93FB

FASTA39843,606
        10         20         30         40         50         60 
MISYSLPNER PNDFSRVIPV VRDIIESVKA RGDNALYQLT EKLDKVKINN IKVSEEELKT 

        70         80         90        100        110        120 
QASKLDPKVK QAIDVAYEQL KAFHEMLVPP NIGGGYQGIS FGVVWRSIEK IGIYVPSGKY 

       130        140        150        160        170        180 
SYPSTLLMAG IPAKVAKVKE IYVASPPNQE GSVNPALAYV AIKLGVNDVY KVGGAQAIAA 

       190        200        210        220        230        240 
LAYGTESVRK VYKIVGPGNV YVQAAKFLVS NVVGIDGIEG PTELVIIADE TAKAEHVVLD 

       250        260        270        280        290        300 
MKAQAEHGPD TYIVLLSNDD ELLKKVEEKI MDDKKIYYII KTKNIDEAIE IANKIAPEHL 

       310        320        330        340        350        360 
SLYVKDAYTL MDKIVNAGAI SLGNTPPAII DYVAGPNHIL PTNGWARIRG GVTVYDFIKP 

       370        380        390 
TMYANVRDIN KQLLEASISL ANYEGFVIHG KSIGVRYE

« Hide

References

[1]"Biogeography of the Sulfolobus islandicus pan-genome."
Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.
Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y.N.15.51 / Yellowstone #2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001404 Genomic DNA. Translation: ACP48392.1.
RefSeqYP_002840314.1. NC_012623.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING419942.YN1551_1297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP48392; ACP48392; YN1551_1297.
GeneID7810082.
KEGGsin:YN1551_1297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0141.
HOGENOMHOG000243914.
KOK00013.
OMAFHRQRVP.
ProtClustDBPRK00877.

Enzyme and pathway databases

BioCycSISL419942:GHVO-1391-MONOMER.
UniPathwayUPA00031; UER00014.

Family and domain databases

HAMAPMF_01024. HisD.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR001692. Histidinol_DH_CS.
IPR022695. Histidinol_DH_monofunct.
IPR012131. Hstdl_DH.
[Graphical view]
PfamPF00815. Histidinol_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000099. Histidinol_dh. 1 hit.
PRINTSPR00083. HOLDHDRGNASE.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00069. hisD. 1 hit.
PROSITEPS00611. HISOL_DEHYDROGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC3NGY2_SULIN
AccessionPrimary (citable) accession number: C3NGY2
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: May 1, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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