A9KP81 (HEM11_CLOPH) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › Clostridium phytofermentans

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087
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. HAMAP-Rule MF_00087
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. HAMAP-Rule MF_00087
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	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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 HAMAP-Rule MF_00087		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 [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]. Strain: ATCC 700394 / DSM 18823 / ISDg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000885 Genomic DNA. Translation: ABX41743.1.
RefSeq	YP_001558482.1. NC_010001.1.
3D structure databases
ProteinModelPortal	A9KP81.
ModBase	Search...
Protein-protein interaction databases
STRING	357809.Cphy_1368.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABX41743; ABX41743; Cphy_1368.
GeneID	5742318.
KEGG	cpy:Cphy_1368.
PATRIC	19502358. VBICloPhy16213_1418.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000069583.
KO	K02492.
OMA	KCVLINT.
ProtClustDB	CLSK984037.
Enzyme and pathway databases
BioCyc	CPHY357809:GHCL-1452-MONOMER.
UniPathway	UPA00251; UER00316.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00087. Glu-tRNA_reductase.
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Pfam	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
SUPFAM	SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit. SSF69742. GlutR. 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:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program