NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
DOI=10.1093/nar/28.21.4317; PubMed=11058132 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis.";
Nucleic Acids Res. 28:4317-4331(2000).

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

BA000004; BAB06767.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H84030; H84030.

RefSeq

NP_243914.1; -.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

Q9K8F8.

Enzyme and pathway databases

BioCyc

BHAL272558:BH3048-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

890506; -.

BA000004_GR; BH3048.

bha:BH3048; -.

fig|272558.1.peg.3048; -.

Phylogenomic databases

HOGENOM

Q9K8F8; -.

Genome annotation databases

CMR

Q9K8F8; BH3048.

Other

ProtoNet

Q9K8F8.

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`	`1 459`	`459`	`Glutamyl-tRNA reductase.`	`PRO_0000113992`
`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: 459 AA [This is the length of the unprocessed precursor]

Molecular weight: 52311 Da [This is the MW of the unprocessed precursor]

CRC64: 37D3F9584579316B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHILMIGLNY KTAPVEIREK FSFQDSELPQ ALHQLRQMKS ILECTIVSTC NRTELYVVAD 

        70         80         90        100        110        120 
QLHTGRHFTK TFLADWFKLP KDEFTPFLTI RENDHAIEHL FRVVTGLDSM ILGETQILGQ 

       130        140        150        160        170        180 
VRNSFFIAQE EQVTGSIFNH LFKQAITLAK RAHSETDIGQ NAVSVSYAAV ELGKKIFDDF 

       190        200        210        220        230        240 
KGKQVLILGA GKMGELTAKH LHSNGAEQVT VINRTREKAA ELAKRFLGVD RPYNELTEAI 

       250        260        270        280        290        300 
VEADILISST GATGYVVTSD MVSHALKKRK GRPLFMVDIA VPRDLDPALA SHDDVYLYDI 

       310        320        330        340        350        360 
DDLQNIVQTN LEERRTEAEK IELLIEEELV EFKQWLNTLG VVPIITALRT KALTVQGETM 

       370        380        390        400        410        420 
ESIERKLPNL TEREKKVLRK HTKSIVNQLL RDPITRIKEL ANAPEREEAL DLFTKIFALE 

       430        440        450 
EELAEQEKQE KVKQAEQEWL AKKRPITCME KQSHVMVKS

Q9K8F8 in FASTA format

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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