hemA1

Functionⁱ

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (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)	Length	Description
Active siteⁱ	46 – 46	1	NucleophileUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087
Siteⁱ	93 – 93	1	Important for activityUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087
Binding siteⁱ	103 – 103	1	SubstrateUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087
Binding siteⁱ	114 – 114	1	SubstrateUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Nucleotide bindingⁱ	183 – 188	6	NADPUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087

Enzyme and pathway databases

BioCycⁱ	CPHY357809:GHCL-1410-MONOMER.
UniPathwayⁱ	UPA00251; UER00316.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamyl-tRNA reductase 1UniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087 (EC:1.2.1.70UniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087 ) Short name: GluTR 1UniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087
Gene namesⁱ	Name:hemA1UniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087 Ordered Locus Names:Cphy_1368
Organismⁱ	Clostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Lachnoclostridium 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)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 403	403	Glutamyl-tRNA reductase 1		PRO_0000335023	Add BLAST

Interactionⁱ

Subunit structureⁱ

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGⁱ	357809.Cphy_1368.

STRINGⁱ

357809.Cphy_1368.

Structureⁱ

3D structure databases

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

Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	45 – 48	4	Substrate bindingUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087
Regionⁱ	108 – 110	3	Substrate bindingUniRule annotation Manual assertion according to rulesⁱ HAMAP-Rule:MF_00087

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.
KOⁱ	K02492.
OMAⁱ	SSAMMLV.
OrthoDBⁱ	POG091H05DA.

Family and domain databases

Gene3Dⁱ	3.40.50.720. 1 hit.
HAMAPⁱ	MF_00087. Glu_tRNA_reductase. 1 hit.
InterProⁱ	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]
Pfamⁱ	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
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.
PATRICⁱ	19502358. VBICloPhy16213_1418.

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.
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.
PATRICⁱ	19502358. VBICloPhy16213_1418.

Phylogenomic databases

eggNOGⁱ	ENOG4105C7E. Bacteria. COG0373. LUCA.
HOGENOMⁱ	HOG000069583.
KOⁱ	K02492.
OMAⁱ	SSAMMLV.
OrthoDBⁱ	POG091H05DA.

Enzyme and pathway databases

UniPathwayⁱ	UPA00251; UER00316.
BioCycⁱ	CPHY357809:GHCL-1410-MONOMER.

Family and domain databases

Gene3Dⁱ	3.40.50.720. 1 hit.
HAMAPⁱ	MF_00087. Glu_tRNA_reductase. 1 hit.
InterProⁱ	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]
Pfamⁱ	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
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_CLOPH

Accessionⁱ

Primary (citable) accession number: A9KP81

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	September 7, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Miscellaneousⁱ

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

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

PATHWAY comments
Index of metabolic and biosynthesis pathways
SIMILARITY comments
Index of protein domains and families

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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - A9KP81 (HEM11_CLOPH)

UniProt

A9KP81 - HEM11_CLOPH

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Glutamyl-tRNA reductase 1

Select a section on the left to see content.

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

<p>Describes the metabolic pathway(s) associated with a protein.</p><p><a href='../manual/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><p><a href='../manual/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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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

Molecule processing

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

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

Region

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>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><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/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>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

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

Miscellaneous

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