hemA1

Functionⁱ

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

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.UniRule annotation

Catalytic activityⁱ

L-glutamate 1-semialdehyde + NADP⁺ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayⁱ: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Glutamyl-tRNA reductase 1 (hemA1), Glutamyl-tRNA reductase 2 (hemA2)
Glutamate-1-semialdehyde 2,1-aminomutase 2 (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1)

This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	46	NucleophileUniRule annotation	1
Siteⁱ	93	Important for activityUniRule annotation	1
Binding siteⁱ	103	SubstrateUniRule annotation	1
Binding siteⁱ	114	SubstrateUniRule annotation	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	183 – 188	NADPUniRule annotation		6

GO - Molecular functionⁱ

glutamyl-tRNA reductase activity Source: UniProtKB-EC
NADP binding Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

Complete GO annotation...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Porphyrin biosynthesis
Ligand	NADP

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00316.

UniPathwayⁱ

UPA00251; UER00316.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation) Short name: GluTR 1UniRule annotation
Gene namesⁱ	Name:hemA1UniRule annotation Ordered Locus Names:Cphy_1368
Organismⁱ	Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Clostridium phytofermentans)
Taxonomic identifierⁱ	357809 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Clostridia › Clostridiales › Lachnospiraceae › Lachnoclostridium › Lachnoclostridium phytofermentans
Proteomesⁱ	UP000000370 Componentⁱ: Chromosome

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000335023	1 – 403	Glutamyl-tRNA reductase 1Add BLAST		403

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGⁱ	357809.Cphy_1368.

STRINGⁱ

357809.Cphy_1368.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	A9KP81.
SMRⁱ	A9KP81.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	45 – 48	Substrate bindingUniRule annotation		4
Regionⁱ	108 – 110	Substrate bindingUniRule annotation		3

Domainⁱ

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.UniRule annotation

Sequence similaritiesⁱ

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105C7E. Bacteria. COG0373. LUCA.
HOGENOMⁱ	HOG000069583.
KEGG Orthology (KO) More...KOⁱ	K02492.
OMAⁱ	FAFKCAA.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H05DA.

Family and domain databases

HAMAPⁱ	MF_00087. Glu_tRNA_reductase. 1 hit.
InterProⁱ	View protein in 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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit.
PIRSFⁱ	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMⁱ	SSF51735. SSF51735. 1 hit. SSF69075. SSF69075. 1 hit. SSF69742. SSF69742. 1 hit.
TIGRFAMsⁱ	TIGR01035. hemA. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

A9KP81-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLGIDHNKAS IEEREIFSFT KKMAADVLLN IKEIEGINGC IILSTCNRME 
        60         70         80         90        100
VWVSCFEEFE TSIYEILCSI KKVDDNRYRH CFIERGGYDA IEHLFYMTCG 
       110        120        130        140        150
LKSKIIGEDQ ILTQVREALE LSRENYCTDS VLETLFRFAI TSAKQVKTQI 
       160        170        180        190        200
HLSVVNSSVI HHVVHELKLS NYLFKGKKCL VIGNGEMGKL AATKLEEEGS 
       210        220        230        240        250
DVTVTVRQYR SGIIEIPVGC NRINYGDRLE HIVEYDFVIS ATSSPNMTIH 
       260        270        280        290        300
LEQLSNLEFK KPVLFIDLAV PRDIDPRITE LKNITLYDID HFKVETVSDE 
       310        320        330        340        350
MKTQLRQIDE ILKTKMDEFI SWYECRGIIK VVQTLSENAA IDVGLRIDKT 
       360        370        380        390        400
MKKIEMDSND KELLAATVHS ATNKVVSKLM FGLRDHVSAA TFQECMVALK 

NIY

Length:403

Mass (Da):46,029

Last modified:February 5, 2008 - v1

Checksum:ⁱ497F1715C4F6418F

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000885 Genomic DNA. Translation: ABX41743.1.

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

CP000885 Genomic DNA. Translation: ABX41743.1.

Genome annotation databases

EnsemblBacteriaⁱ	ABX41743; ABX41743; Cphy_1368.
KEGGⁱ	cpy:Cphy_1368.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CP000885 Genomic DNA. Translation: ABX41743.1.

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

CP000885 Genomic DNA. Translation: ABX41743.1.

3D structure databases

ProteinModelPortalⁱ	A9KP81.
SMRⁱ	A9KP81.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

STRINGⁱ	357809.Cphy_1368.

STRINGⁱ

357809.Cphy_1368.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	ABX41743; ABX41743; Cphy_1368.
KEGGⁱ	cpy:Cphy_1368.

Phylogenomic databases

eggNOGⁱ	ENOG4105C7E. Bacteria. COG0373. LUCA.
HOGENOMⁱ	HOG000069583.
KEGG Orthology (KO) More...KOⁱ	K02492.
OMAⁱ	FAFKCAA.
Database of Orthologous Groups More...OrthoDBⁱ	POG091H05DA.

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00316.

UniPathwayⁱ

UPA00251; UER00316.

Family and domain databases

HAMAPⁱ	MF_00087. Glu_tRNA_reductase. 1 hit.
InterProⁱ	View protein in 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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit.
PIRSFⁱ	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMⁱ	SSF51735. SSF51735. 1 hit. SSF69075. SSF69075. 1 hit. SSF69742. SSF69742. 1 hit.
TIGRFAMsⁱ	TIGR01035. hemA. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HEM11_LACP7
Accessionⁱ	A9KP81Primary (citable) accession number: A9KP81
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
	Last sequence update:	February 5, 2008
	Last modified:	June 7, 2017
	This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - A9KP81 (HEM11_LACP7)

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Glutamyl-tRNA reductase 1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protoporphyrin-IX biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: protoporphyrin-IX biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ