B8I0Q5 (B8I0Q5_CLOCE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase HAMAP MF_00087
Short name=GluTR HAMAP MF_00087
EC=1.2.1.70 HAMAP MF_00087

Gene names

Name:	hemA HAMAP MF_00087
Ordered Locus Names:	Ccel_1274

Organism

Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) [Complete proteome] [HAMAP]

Taxonomic identifier

394503 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	336 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 MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Subunit structure	Homodimer By similarity. HAMAP MF_00087
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 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 MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family. HAMAP MF_00087 RuleBase RU000584

Ontologies

Keywords
Biological process	Porphyrin biosynthesis HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Ligand	NADP HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Molecular function	Oxidoreductase HAMAP MF_00087 RuleBase RU000584 SAAS SAAS018214
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	porphyrin-containing compound 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
Regions
	Nucleotide binding	187 – 192	6	NADP By similarity HAMAP MF_00087
	Region	49 – 52	4	Substrate binding By similarity HAMAP MF_00087
	Region	113 – 115	3	Substrate binding By similarity HAMAP MF_00087
Sites
	Active site	50	1	Nucleophile By similarity HAMAP MF_00087
	Binding site	108	1	Substrate By similarity HAMAP MF_00087
	Binding site	119	1	Substrate By similarity HAMAP MF_00087
	Site	98	1	Important for activity By similarity HAMAP MF_00087

Sequences

	Sequence		Length	Mass (Da)
	B8I0Q5 [UniParc]. Last modified March 3, 2009. Version 1. Checksum: E65A74448FA1F1E7	FASTA	336	37,938
	10 20 30 40 50 60 MTIISASLDY KSAAIDVREK FSYTSTKIRE ILKNIKAVDG VSGAVLLCTC NRTEVYISGE 70 80 90 100 110 120 NIENLNPAMF LCRMSGFIDH KLLMPLFSIR CDSESIFHLM EVACGLQSMV LFEEQIITQV 130 140 150 160 170 180 KHAAAIAREE KTIDSTLETL FRLSITAAKK AKTEVKVKAV PTSAAESAVS ELSKKYCFTH 190 200 210 220 230 240 KKVLVIGNGE IGRLCCKKLL ELGADLTITL RKYKHGEIIV PVGCNTISYD EREGFLSCAD 250 260 270 280 290 300 VVISATTSPH FTITRDMVEK HQRKPEFFID LALPRDIEPE ISKIEGVESY NLDRFCTDFS 310 320 330 VLNHKEVRKI REVIYGFILQ FEKWENYRKE AGLIKE

References

[1]

"Complete sequence of Clostridium cellulolyticum H10." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. , Ivanova N., Zhou J., Richardson P. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35319 / DSM 5812 / JCM 6584 / H10.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001348 Genomic DNA. Translation: ACL75630.1.
RefSeq	YP_002505610.1. NC_011898.1.
3D structure databases
ProteinModelPortal	B8I0Q5.
ModBase	Search...
Protein-protein interaction databases
STRING	B8I0Q5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7310067.
GenomeReviews	Gene locus Ccel_1274 in contig CP001348_GR.
KEGG	cce:Ccel_1274.
PATRIC	19433385. VBICloCel57783_1315.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG305774.
OMA	KETIFRR.
ProtClustDB	CLSK965165.
Family and domain databases
HAMAP	MF_00087. Glu_tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. Pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K02492.
Pfam	PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
SUPFAM	SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. HemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

B8I0Q5_CLOCE

Accession

Primary (citable) accession number: B8I0Q5

Entry history

Integrated into UniProtKB/TrEMBL:	March 3, 2009
Last sequence update:	March 3, 2009
Last modified:	December 14, 2011
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)