NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) 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

CP000512; ABM34211.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_971985.1; -.

3D structure databases

ModBase

A1TTC3.

Ontologies

GO:0008883;	Molecular function: glutamyl-tRNA reductase activity (inferred from electronic annotation from HAMAP).
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.
IPR006162; Ppantne_S.
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

4665154; -.

GenomeReviews

CP000512_GR; Aave_3663.

KEGG

aav:Aave_3663; -.

NMPDR

fig|397945.5.peg.3129; -.

CMR

A1TTC3; Aave_3663.

Other

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_0000335001`
`NP_BIND`	`193 198`	`6`	`NADP (By similarity).`
`REGION`	`55 58`	`4`	`Substrate binding (By similarity).`
`REGION`	`118 120`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`56 56`		`Nucleophile (By similarity).`
`BINDING`	`113 113`		`Substrate (By similarity).`
`BINDING`	`124 124`		`Substrate (By similarity).`
`SITE`	`103 103`	`1`	`Important for activity (By similarity).`

Sequence information

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

Molecular weight: 46734 Da [This is the MW of the unprocessed precursor]

CRC64: F1AF378B845BE924 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVWALGINH TTAPLDLRGR FAFAIDQIAP TLQGLRQSLG GATRHPQVET AILSTCNRTE 

        70         80         90        100        110        120 
IYCAGQQPAL DHTLDWLAHS GGVSPSLLRS HSYTLEESLV ARHAFRVASG LDSMVLGEAQ 

       130        140        150        160        170        180 
ILGQMKDAVR AAETAGALGT TLNQLFQRSF AVAKEVRTST EIGAHSISMA AAAVRLAGQL 

       190        200        210        220        230        240 
FEDLTEIRIL FVGAGEMIEL AATHFAAKNP KSLAIANRTL ERGEKLASRF GGEVMRLADL 

       250        260        270        280        290        300 
PDRLHEFDAV VSCTASSLPI IGLGAVERAL KKRRHRPMFM VDLAVPRDIE PEVKALEDIY 

       310        320        330        340        350        360 
LYTVDDLASV VQTAQASRQA AVAQAEAIID AGVQSFMHWM DQRSPVGGVV PLIQQIHAQA 

       370        380        390        400        410        420 
DEWRALEIAR AKKLIARGED MDAVLEALSR GLTQKMLHGT LAELRAGDAD TRAQTAQTVS 

       430 
RLFLRSQSRS GL

A1TTC3 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