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UniProtKB/Swiss-Prot entry Q2FTC2

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

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Entry information
Entry name NADM_METHJ
Primary accession number Q2FTC2
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on March 21, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 17)
Name and origin of the protein
Protein name Nicotinamide-nucleotide adenylyltransferase
Synonyms EC 2.7.7.1
NAD(+) pyrophosphorylase
NAD(+) diphosphorylase
NMN adenylyltransferase
Gene name
OrderedLocusNames: Mhun_2915
From
Methanospirillum hungatei (strain JF-1 / DSM 864) [TaxID: 323259] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.;
"Complete sequence of Methanospirillum hungatei JF-1.";
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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
CP000254; ABD42607.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_504326.1; -.
3D structure databases
ModBase Q2FTC2.
Enzyme and pathway databases
BioCyc MHUN323259:MHUN_2915-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0000309; Molecular function: nicotinamide-nucleotide adenylyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00243; -; 1.
PBIL [Tree]
InterPro IPR004821; Cyt_trans_rel.
IPR004820; Cytidylyltransf.
IPR006418; NMN_Atrans_arc.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF01467; CTP_transf_2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01527; arch_NMN_Atrans; 1.
TIGR00125; cyt_tran_rel; 1.
ProtoNet Q2FTC2.
Genome annotation databases
GeneID 3924686; -.
GenomeReviews CP000254_GR; Mhun_2915.
KEGG mhu:Mhun_2915; -.
NMPDR fig|323259.5.peg.3052; -.
Phylogenomic databases
HOGENOM Q2FTC2; -.
Genome annotation databases
CMR Q2FTC2; Mhun_2915.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; NAD; Nucleotidyltransferase; Pyridine nucleotide biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom To Length Description FTId
CHAIN   1   174  174     Nicotinamide-nucleotide adenylyltransferase. PRO_1000005736
Sequence information
Length: 174 AA [This is the length of the unprocessed precursor] Molecular weight: 19600 Da [This is the MW of the unprocessed precursor] CRC64: 27A3B19830D21921 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIRALYIGRF QPYHNGHHYV INQIAQEADE LIIGIGSAQM SHEPADPFTA GERVLMITGA 

        70         80         90        100        110        120 
LQDLHKPLYV IPLEDINRNV LWVSHVRAMT PPFHRIYSGN PLVIRLFHEA GIEVLSPAMY 

       130        140        150        160        170 
ERATLSGTKI RDLIACDKPW EDFVPPAVVR VIQEIDGISR IRALNQDDGD CPGR
Q2FTC2 in FASTA format

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