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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway: 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

BioCyciPAER178306:GCEO-399-MONOMER.
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:PAE0594
OrganismiPyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Taxonomic identifieri178306 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000002439 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120488Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei258 – 2581N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi178306.PAE0594.

Structurei

3D structure databases

ProteinModelPortaliQ8ZYW1.
SMRiQ8ZYW1. Positions 1-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiQ8ZYW1.
KOiK01845.
OMAiCGHAHPE.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
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.

Q8ZYW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFERAKSVF PGGVNSPARA LKHLPSPLVA KAASGAYLYT DRGKLVDYCM
60 70 80 90 100
AFGAIILGHA HPRVKKAVEE QLEKGWIYAL LTEQEVEFAE RIRRHMPSVE
110 120 130 140 150
KMRIVNTGTE ATMSAIRAAR GYTKRDVIIK FEGNFHGSHD YVLVKAGSGA
160 170 180 190 200
ATWGIPTSAG IPQEVARLTV VVPYNDIDAF IKAVREVGDR LAAVIVEPVA
210 220 230 240 250
GNYGLIIPDV EFLKALREET QRAGALLIFD EVITGFRVGL GGAQGLFGIR
260 270 280 290 300
PDLTTLGKVV GGGFPIGIFG GRGEVMDLVA PSGPVYNAGT YNAHPVSIAA
310 320 330 340 350
GLAVLKELET GEPYRIANEA AERLAKGVED VAGRLGFDVV VKRMASMFQF
360 370 380 390 400
YFKKGDVKTP QDVRESNEKM YLKLHEIALK HGVYLTPSQY EVNFTSAAHG
410 420
REVVEETLAA LEKSFQELQR EIG
Length:423
Mass (Da):46,016
Last modified:March 1, 2002 - v1
Checksum:i3AEB230212615027
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL62882.1.
RefSeqiNP_558700.1. NC_003364.1.
WP_011007354.1. NC_003364.1.

Genome annotation databases

EnsemblBacteriaiAAL62882; AAL62882; PAE0594.
GeneIDi1465106.
KEGGipai:PAE0594.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009441 Genomic DNA. Translation: AAL62882.1.
RefSeqiNP_558700.1. NC_003364.1.
WP_011007354.1. NC_003364.1.

3D structure databases

ProteinModelPortaliQ8ZYW1.
SMRiQ8ZYW1. Positions 1-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi178306.PAE0594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL62882; AAL62882; PAE0594.
GeneIDi1465106.
KEGGipai:PAE0594.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiQ8ZYW1.
KOiK01845.
OMAiCGHAHPE.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciPAER178306:GCEO-399-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
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...

Publicationsi

  1. "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum."
    Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I., Miller J.H.
    Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827.

Entry informationi

Entry nameiGSA_PYRAE
AccessioniPrimary (citable) accession number: Q8ZYW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2002
Last modified: April 29, 2015
This is version 89 of the entry and version 1 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

External Data

Dasty 3

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 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.