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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia sp. 383.";
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity).
CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP⁺ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2 .
SUBUNIT: Homodimer (By similarity).
DOMAIN: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization (By similarity).
MISCELLANEOUS: During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA (By similarity).
SIMILARITY: Belongs to the glutamyl-tRNA 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

CP000151; ABB07199.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_367843.1; -.

3D structure databases

ModBase

Q39K17.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_A3598-MON; -.

Ontologies

GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0006779;	Biological process: porphyrin biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00087; -; 1.
PBIL [Tree]

InterPro

IPR000343; 4pyrrol_synth_GluRdtase.
IPR015896; 4pyrrol_synth_GluRdtase_C.
IPR015895; 4pyrrol_synth_GluRdtase_N.
IPR016040; NAD(P)-bd.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Gene3D

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

Pfam

PF00745; GlutR_dimer; 1.
PF05201; GlutR_N; 1.
PF01488; Shikimate_DH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000445; 4pyrrol_synth_GluRdtase; 1.

TIGR01035; hemA; 1.

PS00747; GLUTR; 1.

Genome annotation databases

GeneID

3748776; -.

GenomeReviews

CP000151_GR; Bcep18194_A3598.

KEGG

bur:Bcep18194_A3598; -.

NMPDR

fig|269483.3.peg.4990; -.

Phylogenomic databases

HOGENOM

Q39K17; -.

Genome annotation databases

CMR

Q39K17; Bcep18194_A3598.

Other

ProtoNet

Q39K17.

UniRef

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

Keywords

Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 432`	`432`	`Glutamyl-tRNA reductase.`	`PRO_1000004600`
`NP_BIND`	`194 199`	`6`	`NADP (By similarity).`
`REGION`	`55 58`	`4`	`Substrate binding (By similarity).`
`REGION`	`119 121`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`56 56`		`Nucleophile (By similarity).`
`BINDING`	`114 114`		`Substrate (By similarity).`
`BINDING`	`125 125`		`Substrate (By similarity).`
`SITE`	`104 104`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 47477 Da [This is the MW of the unprocessed precursor]

CRC64: F67F235CF452D15B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQLLTIGINH HTAPVALRER VAFPLEQIKP ALVTFKNVFL GPQAPNTPEA AILSTCNRTE 

        70         80         90        100        110        120 
LYCATDDRAA REGAVRWLSE YHRIPVDELA PHVYALPQSE AVRHAFRVAS GLDSMVLGET 

       130        140        150        160        170        180 
QILGQMKDAV RTATEAGALG TYLNQLFQRT FAVAKEVRGT TEIGTQSVSM AAAAVRLAQR 

       190        200        210        220        230        240 
IFEKVSDQRV LFIGAGEMIE LCATHFAAQG PRELVVANRT AERGQRLAER FNGRAMPLAD 

       250        260        270        280        290        300 
LPTRMHEFDI IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGKLKDV 

       310        320        330        340        350        360 
FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDTRSVVPVI RHMHTQADAL 

       370        380        390        400        410        420 
RRAEVDKAQK LLARGDDPAA VLEALSQALT NKLIHGPTSA LNRVNGADRD SLIDLMRGFY 

       430 
QHAPRSNDQS GH

Q39K17 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