Reviewed, UniProtKB/Swiss-Prot A9KP81 (HEM11_CLOPH)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 1
      Short name=GluTR 1
    EC=1.2.1.70

Gene names

Name:	hemA1
Ordered Locus Names:	Cphy_1368

Organism

Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) [Complete proteome] [HAMAP]

Taxonomic identifier

357809 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 structure	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.
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Glutamyl-tRNA reductase 1		PRO_0000335023
Regions
	Nucleotide binding	183 – 188	6	NADP By similarity
	Region	45 – 48	4	Substrate binding By similarity
	Region	108 – 110	3	Substrate binding By similarity
Sites
	Active site	46	1	Nucleophile By similarity
	Binding site	103	1	Substrate By similarity
	Binding site	114	1	Substrate By similarity
	Site	93	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9KP81-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 497F1715C4F6418F	FASTA	403	46,029
	10 20 30 40 50 60 MLGIDHNKAS IEEREIFSFT KKMAADVLLN IKEIEGINGC IILSTCNRME VWVSCFEEFE 70 80 90 100 110 120 TSIYEILCSI KKVDDNRYRH CFIERGGYDA IEHLFYMTCG LKSKIIGEDQ ILTQVREALE 130 140 150 160 170 180 LSRENYCTDS VLETLFRFAI TSAKQVKTQI HLSVVNSSVI HHVVHELKLS NYLFKGKKCL 190 200 210 220 230 240 VIGNGEMGKL AATKLEEEGS DVTVTVRQYR SGIIEIPVGC NRINYGDRLE HIVEYDFVIS 250 260 270 280 290 300 ATSSPNMTIH LEQLSNLEFK KPVLFIDLAV PRDIDPRITE LKNITLYDID HFKVETVSDE 310 320 330 340 350 360 MKTQLRQIDE ILKTKMDEFI SWYECRGIIK VVQTLSENAA IDVGLRIDKT MKKIEMDSND 370 380 390 400 KELLAATVHS ATNKVVSKLM FGLRDHVSAA TFQECMVALK NIY

References

[1]

"Complete genome sequence of Clostridium phytofermentans ISDg." Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L., LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C. , Han C., Kuske C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.A., Richardson P. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000885 Genomic DNA. Translation: ABX41743.1.
RefSeq	YP_001558482.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5742318.
GenomeReviews	Gene locus Cphy_1368 in contig CP000885_GR.
KEGG	cpy:Cphy_1368.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM11_CLOPH

Accession

Primary (citable) accession number: A9KP81

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	November 25, 2008
This is version 11 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)