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P73138 (FRMA_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-(hydroxymethyl)glutathione dehydrogenase

EC=1.1.1.284
Alternative name(s):
Alcohol dehydrogenase class-3
EC=1.1.1.1
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase
Short name=FALDH
Short name=FDH
Short name=GSH-FDH
EC=1.1.1.-
Gene names
Name:frmA
Ordered Locus Names:sll0990
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processethanol oxidation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionS-(hydroxymethyl)glutathione dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

alcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369S-(hydroxymethyl)glutathione dehydrogenase
PRO_0000160778

Sites

Metal binding401Zinc 1; catalytic By similarity
Metal binding621Zinc 1; catalytic By similarity
Metal binding921Zinc 2 By similarity
Metal binding951Zinc 2 By similarity
Metal binding981Zinc 2 By similarity
Metal binding1061Zinc 2 By similarity
Metal binding1691Zinc 1; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
P73138 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C8A337424F2F1680

FASTA36939,211
        10         20         30         40         50         60 
MKSRAAVAFE VGKPLQIVEI DVAPPQQGEV LVKITHTGVC HTDAFTLSGD DPEGLFPVVL 

        70         80         90        100        110        120 
GHEGAGIVVE VGEGVTSVQL GDHVIPLYTA ECGKCLFCRS GKTNLCVAVR ATQGKGVMPD 

       130        140        150        160        170        180 
GTSRFSYNGQ SLYHYMGCST FSEYTVVAEV SLAKINPEAN HEHVCLLGCG VTTGIGAVHN 

       190        200        210        220        230        240 
TAKVQPGDSV AVFGLGGIGL AVVQGARQAK AGRIIAIDTN PAKFELAKQM GATDCINPKD 

       250        260        270        280        290        300 
HDQPIQQVIV EMTGWGVDHS FECIGNVEVM RSALECAHRG WGQSVIIGVA GAGQEISTRP 

       310        320        330        340        350        360 
FQLVTGRKWM GTAFGGVKGR SQLPGMVEQS MRGEIQLAPF VTHTMELKDI NQAFDLMHDG 


KSIRSVIHY 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA17164.1.
PIRS75250.
RefSeqNP_440484.1. NC_000911.1.
YP_005650542.1. NC_017277.1.
YP_007450368.1. NC_020286.1.

3D structure databases

ProteinModelPortalP73138.
SMRP73138. Positions 1-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.sll0990.

Proteomic databases

PaxDbP73138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA17164; BAA17164; BAA17164.
GeneID12256233.
14616017.
953785.
KEGGsyn:sll0990.
syy:SYNGTS_0589.
syz:MYO_15950.
PATRIC23838146. VBISynSp132158_0641.

Phylogenomic databases

eggNOGCOG1062.
KOK00121.
OMAAWKSGAP.
OrthoDBEOG6K9QDH.
PhylomeDBP73138.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 2 hits.
TIGRFAMsTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFRMA_SYNY3
AccessionPrimary (citable) accession number: P73138
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families