NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Nelson K.E.;
"Complete genome sequence of Campylobacter hominis ATCC BAA-381, a commensal isolated from the human gastrointestinal tract.";
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

CP000776; ABS52226.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001406458.1; -.

3D structure databases

ModBase

A7I1R7.

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

5408761; -.

GenomeReviews

CP000776_GR; CHAB381_0896.

KEGG

cha:CHAB381_0896; -.

NMPDR

fig|360107.5.peg.879; -.

CMR

A7I1R7; CHAB381_0896.

Other

ProtoNet

A7I1R7.

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`	`1 429`	`429`	`Glutamyl-tRNA reductase.`	`PRO_1000057572`
`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: 429 AA [This is the length of the unprocessed precursor]

Molecular weight: 47896 Da [This is the MW of the unprocessed precursor]

CRC64: 24112E1047B97089 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYMSVSFTH KNTDIIVREK LSFANDVKKR EILKLICSNK AIKECLVLST CNRVEVLAYI 

        70         80         90        100        110        120 
DDFNYTSDYV IKAISKLSGV DFDELKERAD IYEDDGAIHH LFSVASSLDS LVVGETQIVG 

       130        140        150        160        170        180 
QLKDAYNFAK NERKSGVMLD LAINSALKCA AVIRSKTDIS KNPISVASVA VCMAREKIGD 

       190        200        210        220        230        240 
LGGTTAVVVG AGEMAELACK HLITHKAKVI IINRNIDHAK KLAESLGENA SIAEFSNLGE 

       250        260        270        280        290        300 
FINKYALIFS ATGANKPIIT DLLAKPQNFK RYFFDIAVPR DIDITCDDLS EVYAVDDLEE 

       310        320        330        340        350        360 
IVRKNLLLRE EQAQIAYSIV GRETTKFYKD LKTLSSTPII KALRNSAKKV AETELKKAIK 

       370        380        390        400        410        420 
RGYLRHSDID EARKLIHQVF KAFLHTPTVN LKNLDENAQN DINAIAEIFG IEEDFDKFCE 


NSLENKNEI

A7I1R7 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