[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.; "Genome sequence of Campylobacter curvus 525.92 isolated from human feces."; Submitted (JUL-2007) 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

CP000767; EAT99944.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001408389.1; -.

3D structure databases

ModBase

A7GYU7.

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.
IPR002198; DHase_sc/Rdtase_SDR.
IPR016040; NAD(P)-bd.
IPR000010; Prot_inh_cystat.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR19410; ADH_short_C2; 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

5407303; -.

GenomeReviews

CP000767_GR; Ccur92_10850.

KEGG

ccv:CCV52592_0764; -.

CMR

A7GYU7; Ccur92_10850.

Other

ProtoNet

A7GYU7.

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`	`1 428`	`428`	`Glutamyl-tRNA reductase.`	`PRO_0000335020`
`NP_BIND`	`190 195`	`6`	`NADP (By similarity).`
`REGION`	`50 53`	`4`	`Substrate binding (By similarity).`
`REGION`	`115 117`	`3`	`Substrate binding (By similarity).`
`ACT_SITE`	`51 51`		`Nucleophile (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`BINDING`	`121 121`		`Substrate (By similarity).`
`SITE`	`100 100`	`1`	`Important for activity (By similarity).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 47977 Da [This is the MW of the unprocessed precursor]

CRC64: 6B0B44CB6ABDABD0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHYLNISFTY KNTDISVREK LAFDSDEKKD QILRLLKSSK NIIECMVLST CNRVEVLAYT 

        70         80         90        100        110        120 
NDIKSAMTHI IRCLTVYSGV FEDELFERAD IYEDSGAVHH LFAVASSLDS LVVGETQIVG 

       130        140        150        160        170        180 
QLKNAFKFAF DNASSGEHIS RLVHYACKCA ARVRNETQIS KNPISVSSVA VAKAKEIFGT 

       190        200        210        220        230        240 
LENKTAVVIG AGEMGELAAK HLITSGANVI IINRSSDHVE ELVENLGDKA SWDSILKLKE 

       250        260        270        280        290        300 
YINKYDLIFS STSAPHAIIT GELIEPQEFR RYFFDIAVPR DIDLVNTDKI SVYSVDSLEE 

       310        320        330        340        350        360 
MVRRNLALRE EQAQTAYSIV GQSTNEFLKF LKDNISIPLI KTIRKKAEIC AEAELEKALK 

       370        380        390        400        410        420 
KGYLKHSDKE EAAKLIHQVF KAFLHSPTIN LKSLASKNDA EQIAGGIKFL FDIKEENLEN 


LTKDIDEI

A7GYU7 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