[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Ames / isolate Porton; DOI=10.1038/nature01586; PubMed=12721629 [NCBI, ExPASy, EBI, Israel, Japan] Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.; "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."; Nature 423:81-86(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Ames ancestor; Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.; "Bacillus anthracis comparative genomics."; Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Sterne; Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.; "Complete genome sequence of Bacillus anthracis Sterne."; Submitted (JAN-2004) 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

AE016879; AAP28397.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017334; AAT33821.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017225; AAT56661.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_846911.1; -.
YP_021346.1; -.
YP_030610.1; -.

3D structure databases

HSSP

Q9UXR8; 1GPJ. [HSSP ENTRY / PDB]

ModBase

Q81LC5.

Enzyme and pathway databases

BioCyc

BANT260799:BAS4363-MON; -.
BANT261594:GBAA4698-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

1083700; -.
2816103; -.
2852284; -.

GenomeReviews

AE016879_GR; BA_4698.
AE017225_GR; BAS4363.
AE017334_GR; GBAA4698.

KEGG

ban:BA4698; -.
bar:GBAA4698; -.
bat:BAS4363; -.

TIGR

BA_4698; -.
GBAA4698; -.

Phylogenomic databases

HOGENOM

Q81LC5; -.

Other

ProtoNet

Q81LC5.

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`	`1 444`	`444`	`Glutamyl-tRNA reductase.`	`PRO_0000113988`
`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: 444 AA [This is the length of the unprocessed precursor]

Molecular weight: 49825 Da [This is the MW of the unprocessed precursor]

CRC64: 4BB7F3FC998B0643 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHILVVSVNY RTAPVEFREK LTFQAAELER AMTTLQNQKS VLENVIVSTC NRTEIYAVVD 

        70         80         90        100        110        120 
QLHTGRYYIK KFLADWFQLE IEEVAPYLTI FEQDGAIDHL FRVTCGLDSM VVGETQILGQ 

       130        140        150        160        170        180 
IKDSFLEAQQ VKATGTIFNE LFKQVITLAK RAHSETTIGE SAMSVSYAAV ELGKKIFGEL 

       190        200        210        220        230        240 
TDCHVLILGA GKMGELALQN LYGSGARKVT VMNRTLSKAE IMAEKYMGHA KPLSELQCAL 

       250        260        270        280        290        300 
LEADILISST GASDYVITKE MMTKVEKMRS GRPLFMVDIA VPRDIDPAID ELEGSFLYDI 

       310        320        330        340        350        360 
DDLQGVVEAN RAERLKEAEK IQFMIEEEIV LFKTWLSTLG VVPLISALRD KALAIQSETM 

       370        380        390        400        410        420 
ESLERKIPNL SDRERKVISK HTKSIINQLL KDPILVAKEI AAEEGADEKL ALFAKIFDLE 

       430        440 
MEDVESRAEE VEHKRVWTPS VPSL

Q81LC5 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