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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Nitrosopumilus maritimus (strain SCM1)
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

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciNMAR436308:GI3J-510-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:Nmar_0490
OrganismiNitrosopumilus maritimus (strain SCM1)
Taxonomic identifieri436308 [NCBI]
Taxonomic lineageiArchaeaThaumarchaeotaNitrosopumilalesNitrosopumilaceaeNitrosopumilus
ProteomesiUP000000792 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi436308.Nmar_0490.

Structurei

3D structure databases

ProteinModelPortaliA9A1A0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiACLMIEP.

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.

A9A1A0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSKLFSDA KKVIPSGVNS PVRYFEPYPF FTKKANGAYI WDVDNRKLID
60 70 80 90 100
FCNGYGALLL GHRRKEIINS VSKQLTKGTL YCTPTEGETE LAKLIIGNFP
110 120 130 140 150
SIDKVRLMNT GGEATMTAIR LARGFTKKKK IIKFEGCYHG AHDSVLVKAG
160 170 180 190 200
SGSAHNGISV SDGGLDEVSK NTLVVQYNNI EDLQKTIQKN KDIAGVIVEP
210 220 230 240 250
ILANMGLILP EKNFLSDLRK ITKENNIPLI FDEVVTGFRV APGGAQEHFG
260 270 280 290 300
IKPDITTMAK ALSNGFAISA VGGKKEIMDL LSPGGKVYQA STFAGNPISV
310 320 330 340 350
SAAIASIKTI NKLKNKLYSK LERFNLLFST ALDDMATDMG IPHQINFTAS
360 370 380 390 400
MFQIFFTNKP VTNYETSKKA NAKKFQKLFR TLLKKGIFIA PSQFEVVFLS
410 420
DAHTENDLNK TLDAYHLALK SVKN
Length:424
Mass (Da):46,604
Last modified:January 15, 2008 - v1
Checksum:i40046333B8AFB473
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000866 Genomic DNA. Translation: ABX12386.1.
RefSeqiWP_012214873.1. NC_010085.1.
YP_001581824.1. NC_010085.1.

Genome annotation databases

EnsemblBacteriaiABX12386; ABX12386; Nmar_0490.
GeneIDi5774718.
KEGGinmr:Nmar_0490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000866 Genomic DNA. Translation: ABX12386.1.
RefSeqiWP_012214873.1. NC_010085.1.
YP_001581824.1. NC_010085.1.

3D structure databases

ProteinModelPortaliA9A1A0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi436308.Nmar_0490.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX12386; ABX12386; Nmar_0490.
GeneIDi5774718.
KEGGinmr:Nmar_0490.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiACLMIEP.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciNMAR436308:GI3J-510-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCM1.

Entry informationi

Entry nameiGSA_NITMS
AccessioniPrimary (citable) accession number: A9A1A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: January 15, 2008
Last modified: April 1, 2015
This is version 55 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.