NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

Comments

FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA) (By similarity).
CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine + glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate.
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the murCDEF 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

BA000040; BAC51869.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_773244.1; -.

3D structure databases

HSSP

P14900; 1E0D. [HSSP ENTRY / PDB]

ModBase

Q89FU5.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL6604-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0008764;	Molecular function: UDP-N-acetylmuramoylalanine-D-glutamate ligase activity (inferred from electronic annotation from HAMAP).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
GO:0009252;	Biological process: peptidoglycan biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0008360;	Biological process: regulation of cell shape (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00639; -; 1.
PBIL [Tree]

InterPro

IPR013149; AlcDHase_Zn-bd.
IPR004101; Mur_ligase_C.
IPR013221; Mur_ligase_cen.
IPR016040; NAD(P)-bd.
IPR005762; UDP-N-AcMur-Glu_ligase.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.190.20; Mur_ligase_C; 1.
G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00107; ADH_zinc_N; 1.
PF02875; Mur_ligase_C; 1.
PF08245; Mur_ligase_M; 1.
Pfam graphical view of domain structure.

TIGR01087; murD; 1.

Genome annotation databases

GeneID

1051159; -.

GenomeReviews

BA000040_GR; bll6604.

KEGG

bja:bll6604; -.

NMPDR

fig|224911.1.peg.6604; -.

Phylogenomic databases

HOGENOM

Q89FU5; -.

Genome annotation databases

CMR

Q89FU5; bll6604.

Other

UniRef

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

Keywords

ATP-binding; Cell cycle; Cell division; Cell shape; Cell wall biogenesis/degradation; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Peptidoglycan synthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 466`	`466`	`UDP-N-acetylmuramoylalanine--D-glutamate ligase.`	`PRO_0000108980`
`NP_BIND`	`121 127`	`7`	`ATP (Potential).`

Sequence information

Length: 466 AA [This is the length of the unprocessed precursor]

Molecular weight: 48501 Da [This is the MW of the unprocessed precursor]

CRC64: 174A447C5BB25A63 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIPVTSFAGK TVAVFGLGGS GLASCHALKA GGAEVIAADD NAENVAKAAQ AGFITADLRD 

        70         80         90        100        110        120 
VSWAGFAALV LAPGVPLTHP VPHWSVLKAR EAGVEVIGDI ELFCRERRRH APDAPFVAIT 

       130        140        150        160        170        180 
GTNGKSTTTA LIAHLTKVAG YDTQMGGNIG TAILSLEPPR TGRVHVIEMS SYQIDLTPSL 

       190        200        210        220        230        240 
DPSVGILLNV SEDHIDRHGT IAHYAAVKER LVAGVQAGGT SIVGVDDGYC RDIADRLDRA 

       250        260        270        280        290        300 
GKNVVRISVK NPLASGIHVE HGTIVRTAGG ARSEVAKLGG IGSLRGLHNA QNAACAAAAA 

       310        320        330        340        350        360 
LAMGISQDVL QDGLRSFPGL AHRMEQVGRR GNVLFVNDSK GTNADATAHA LSSFADIFWI 

       370        380        390        400        410        420 
AGGKPKAGGI TSLTGFFPRI RKAYLIGEAA QEFSGTLGTQ VAHEISQTLD VAVEHAARDA 

       430        440        450        460 
EASGLTDAVV LLSPACASFD QYRNFEIRGT KFRELVQALP GVKPVV

Q89FU5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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