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UniProtKB/Swiss-Prot entry P14775


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHM2_METEX
Primary accession number P14775
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1990
Sequence was last modified on April 1, 1990 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 65)
Name and origin of the protein
Protein name Methanol dehydrogenase subunit 2 [Precursor]
Synonyms EC 1.1.99.8
MDH small subunit beta
MDH-associated peptide
MEDH
Gene name
Name: moxI
From
Methylobacterium extorquens (Protomonas extorquens) [TaxID: 408] 
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Methylobacteriaceae; Methylobacterium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=AM1 / NCIMB 9133;
PubMed=2504152 [NCBI, ExPASy, EBI, Israel, Japan]
Nunn D.N., Day D., Anthony C.;
"The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1.";
Biochem. J. 260:857-862(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=AM1 / NCIMB 9133;
DOI=10.1093/nar/16.15.7722; PubMed=2842733 [NCBI, ExPASy, EBI, Israel, Japan]
Nunn D.N., Anthony C.;
"The nucleotide sequence and deduced amino acid sequence of the genes for cytochrome cL and a hypothetical second subunit of the methanol dehydrogenase of Methylobacterium AM1.";
Nucleic Acids Res. 16:7722-7722(1988).
[3]
DISULFIDE BONDS.
DOI=10.1038/nsb0294-102; PubMed=7656012 [NCBI, ExPASy, EBI, Israel, Japan]
Blake C.C.F., Ghosh M., Harlos K., Avezoux A., Anthony C.;
"The active site of methanol dehydrogenase contains a disulphide bridge between adjacent cysteine residues.";
Nat. Struct. Biol. 1:102-105(1994).
[4]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS).
DOI=10.1016/S0969-2126(01)00148-4; PubMed=7735834 [NCBI, ExPASy, EBI, Israel, Japan]
Ghosh M., Anthony C., Harlos K., Goodwin M.G., Blake C.;
"The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.";
Structure 3:177-187(1995).
[5]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1021/bi002932l; PubMed=11502173 [NCBI, ExPASy, EBI, Israel, Japan]
Afolabi P.R., Mohammed F., Amaratunga K., Majekodunmi O., Dales S.L., Gill R., Thompson D., Cooper J.B., Wood S.P., Goodwin P.M., Anthony C.;
"Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L).";
Biochemistry 40:9799-9809(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X15792; CAA33796.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X07856; CAA30705.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1H4I; X-ray; 1.94 A; B/D=23-96.[ExPASy / RCSB / EBI]
1H4J; X-ray; 3.00 A; B/D/F/H=23-96.[ExPASy / RCSB / EBI]
1W6S; X-ray; 1.20 A; B/D=23-96.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H4I; -.
1H4J; -.
1W6S; -.
ModBase P14775.
Enzyme and pathway databases
BioCyc MetaCyc:MON-3922; -.
Family and domain databases
InterPro IPR003420; Meth_DHase_bsu.
Graphical view of domain structure.
Gene3D G3DSA:4.10.160.10; Meth_DH_beta; 1.
Pfam PF02315; MDH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF029163; Meth_DH_beta; 1.
BLOCKS P14775.
Other
ProtoNet P14775.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Methanol utilization; Oxidoreductase; Periplasm; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
SIGNAL   1   22  22      
CHAIN   23   96  74     Methanol dehydrogenase subunit 2. PRO_0000025569
DISULFID   28   34         
HELIX   56   59  4      
HELIX   61   83  23      
HELIX   90   92  3      
Sequence information
Length: 96 AA [This is the length of the unprocessed precursor] Molecular weight: 10512 Da [This is the MW of the unprocessed precursor] CRC64: 9C082124F26F3159 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKTTLIAAAI VALSGLAAPA LAYDGTKCKA AGNCWEPKPG FPEKIAGSKY DPKHDPKELN 

        70         80         90 
KQADSIKQME ERNKKRVENF KKTGKFEYDV AKISAN 

P14775 in FASTA format

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