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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 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:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:DR_0555
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001204071 – 444Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei278N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

STRINGi243230.DR_0555.

Structurei

3D structure databases

ProteinModelPortaliQ9RWW0.
SMRiQ9RWW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiQ9RWW0.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiPOG091H04O1.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3. 1 hit.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RWW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLSETHPTA RSEALFVRAR AVTPGGVNSP VRAFRSVGGV PRFIASAQGA
60 70 80 90 100
YLTDADGARY LDYIGSWGPM ILGHNHPAVR DAVAQALASG TSFGAPNERE
110 120 130 140 150
VELAELIVEL TGAERVRFVS SGTEATMSAL RLARGYTGRK FIVKFRGNYH
160 170 180 190 200
GHADGLLVEA GSGLLTNAEG DLGAAAPSSA GVPEEYAGLT LVLDYNDPEA
210 220 230 240 250
LDALMAQRGD EIAAVIFEPV VGNAGVLIPT SDFLAALHRV RDFGAVLIAD
260 270 280 290 300
EVMTGFRLSL NGATGLLSLD PDLRCWGKIV GGGLPVGAYG GRADIMDFVS
310 320 330 340 350
PQGPVYQAGT LSGNPLAMAA GIATLRELKA NPGLYRQLDE YAARLAAGLR
360 370 380 390 400
GAAERAGVAV SINHIGSMLT VFFQDAPDGS VRDYAAAARS DTAAFAAWFQ
410 420 430 440
GLLARGIYWA PSQFESIFIS AAHGEPELAA TLEAAAQAFE GVKP
Length:444
Mass (Da):46,305
Last modified:June 1, 2001 - v2
Checksum:i344BFE4E3107A8C8
GO

Sequence cautioni

The sequence AAF10132 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10132.1. Different initiation.
PIRiE75505.
RefSeqiNP_294278.1. NC_001263.1.
WP_010887200.1. NC_001263.1.
WP_027479528.1. NZ_CP015081.1.

Genome annotation databases

EnsemblBacteriaiAAF10132; AAF10132; DR_0555.
GeneIDi1799707.
KEGGidra:DR_0555.
PATRICi21628634. VBIDeiRad64572_0730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10132.1. Different initiation.
PIRiE75505.
RefSeqiNP_294278.1. NC_001263.1.
WP_010887200.1. NC_001263.1.
WP_027479528.1. NZ_CP015081.1.

3D structure databases

ProteinModelPortaliQ9RWW0.
SMRiQ9RWW0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_0555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF10132; AAF10132; DR_0555.
GeneIDi1799707.
KEGGidra:DR_0555.
PATRICi21628634. VBIDeiRad64572_0730.

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiQ9RWW0.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiPOG091H04O1.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3. 1 hit.
InterProiIPR004639. 4pyrrol_synth_GluAld_NH2Trfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSA_DEIRA
AccessioniPrimary (citable) accession number: Q9RWW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.