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., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Chlorobium chlorochromatii CaD3.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: 2,3,4,5-tetrahydrodipicolinate + NAD(P)⁺ = 2,3-dihydrodipicolinate + NAD(P)H.
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 4/4 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the dihydrodipicolinate reductase family.

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

CP000108; ABB29056.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_380099.1; -.

3D structure databases

ModBase

Q3APL9.

Enzyme and pathway databases

BioCyc

CCHL340177:CAG_1805-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008839;	Molecular function: dihydrodipicolinate reductase activity (inferred from electronic annotation from HAMAP).
GO:0019877;	Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00102; -; 1.
PBIL [Tree]

InterPro

IPR000846; DapB.
IPR011770; DapB_bac/pln.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR20836; DapB_bac/pln; 1.

Pfam

PF05173; DapB_C; 1.
PF01113; DapB_N; 1.
Pfam graphical view of domain structure.

ProDom

PD004105; DapB; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR00036; dapB; 1.

PROSITE

PS01298; DAPB; FALSE_NEG.

BLOCKS

Q3APL9.

Genome annotation databases

GeneID

3746920; -.

GenomeReviews

CP000108_GR; Cag_1805.

KEGG

cch:Cag_1805; -.

Phylogenomic databases

HOGENOM

Q3APL9; -.

Genome annotation databases

CMR

Q3APL9; Cag_1805.

Other

ProtoNet

Q3APL9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; Cytoplasm; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 249`	`249`		`Dihydrodipicolinate reductase.`	`PRO_0000228338`

Sequence information

Length: 249 AA [This is the length of the unprocessed precursor]

Molecular weight: 26844 Da [This is the MW of the unprocessed precursor]

CRC64: 550D36B4E9B1706D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFTLIGNGR MGQQVAHIIN NSSAHSIAAI LDVDATITPE VFHGSDAIID FTVRHAFLEN 

        70         80         90        100        110        120 
LPAMVASGVP IVVGTTGWDD VQADVRQQIA AANTSLLYSA NFSLGVNIFM RIVREAARMI 

       130        140        150        160        170        180 
EPFSHFDIAL TEQHHTGKAD FPSGTALRTA QMVLAANSRK TSIVRELADG NKLTPNELHV 

       190        200        210        220        230        240 
ASLRLGTIFG KHSAFIDSET DDIEISHTAK SRSGFAAGAV EAAAWLALRH TTAPGFYTMD 


DFLDEKLGK

Q3APL9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools