NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 509 / IFO 12109;
DOI=10.1042/BJ20021443; PubMed=12408752 [NCBI, ExPASy, EBI, Israel, Japan]
Raux E., Leech H.K., Beck R., Schubert H.L., Santander P.J., Roessner C.A., Scott A.I., Martens J.H., Jahn D., Thermes C., Rambach A., Warren M.J.;
"Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium.";
Biochem. J. 370:505-516(2003).

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

AJ508220; CAD48144.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

Q8GCB0.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004764;	Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
IPR003462; ODC_Mu_crystall.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR13812; ODC_Mu_crystall; 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.

TIGRFAMs

TIGR01035; hemA; 1.

PROSITE

PS00747; GLUTR; 1.

Other

ProtoNet

Q8GCB0.

UniRef

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

Keywords

NADP; Oxidoreductase; Porphyrin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 446`	`446`	`Glutamyl-tRNA reductase.`	`PRO_0000113994`
`NP_BIND`	`189 194`	`6`	`NADP (By similarity).`
`REGION`	`49 52`	`4`	`Substrate binding (By similarity).`
`REGION`	`114 116`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`50 50`		`Nucleophile (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`120 120`		`Substrate (By similarity).`
`SITE`	`99 99`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 446 AA [This is the length of the unprocessed precursor]

Molecular weight: 49838 Da [This is the MW of the unprocessed precursor]

CRC64: 8A86F67822352A02 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHIIAVGLNF RTAPVEIREK LSFNEQELAS AMKTLSGQKS ILENIIVSTC NRTEIYAVVD 

        70         80         90        100        110        120 
QLHTGRYYVK AFLAEWFGID KEEFSPYLTI YENDGAIEHL YRVACGLDSM VIGETQILGQ 

       130        140        150        160        170        180 
VRSSFLLAQE EETIGTVFNQ LFKQAVTLAK KAHHETEIGA NAVSVSYAAV ELAKKIFGDL 

       190        200        210        220        230        240 
SSKHVLILGA GKMGQLAVQN LYGSGAKKVT VVNRTFEKAQ ELANRFSGEA KPFADLQHAL 

       250        260        270        280        290        300 
SEADILISST GANDYVVTKQ MMSEAERTRK GRPLFMVDIA VPRDLDPELD ELETVFLYDI 

       310        320        330        340        350        360 
DDLNGIVESN LQERQKAADE IEIMLEAEIV AFKSWLGTLG VVPVISALRQ KALTIQAETM 

       370        380        390        400        410        420 
KSIDRKLPDL SERERKVLNK HTKSIINQLL RDPIPHAKEL AGEKHAEESL ELFMKIFNIE 

       430        440 
QEVALQKEKE EQLHTSITSH SVAYQS

Q8GCB0 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