Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
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-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Ordered Locus Names:APE_2299.1
OrganismiAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Taxonomic identifieri272557 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum
Proteomesi
  • UP000002518 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001204761 – 429Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266N6-(pyridoxal phosphate)lysineBy similarity1

Interactioni

Protein-protein interaction databases

STRINGi272557.APE_2299.1.

Structurei

Secondary structure

1429
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 14Combined sources10
Turni15 – 17Combined sources3
Helixi19 – 21Combined sources3
Beta strandi22 – 24Combined sources3
Helixi25 – 29Combined sources5
Beta strandi31 – 33Combined sources3
Beta strandi37 – 42Combined sources6
Beta strandi44 – 47Combined sources4
Beta strandi52 – 57Combined sources6
Helixi58 – 60Combined sources3
Helixi70 – 81Combined sources12
Helixi91 – 104Combined sources14
Beta strandi109 – 115Combined sources7
Helixi116 – 131Combined sources16
Beta strandi135 – 140Combined sources6
Helixi148 – 150Combined sources3
Beta strandi151 – 153Combined sources3
Beta strandi163 – 166Combined sources4
Helixi171 – 174Combined sources4
Beta strandi177 – 181Combined sources5
Helixi185 – 195Combined sources11
Helixi196 – 198Combined sources3
Beta strandi199 – 204Combined sources6
Beta strandi206 – 208Combined sources3
Beta strandi210 – 212Combined sources3
Helixi218 – 231Combined sources14
Beta strandi234 – 239Combined sources6
Turni240 – 245Combined sources6
Helixi250 – 255Combined sources6
Beta strandi260 – 265Combined sources6
Helixi266 – 269Combined sources4
Beta strandi275 – 279Combined sources5
Helixi281 – 284Combined sources4
Turni288 – 290Combined sources3
Beta strandi291 – 293Combined sources3
Turni298 – 301Combined sources4
Helixi303 – 318Combined sources16
Helixi321 – 343Combined sources23
Beta strandi347 – 352Combined sources6
Beta strandi355 – 360Combined sources6
Helixi368 – 371Combined sources4
Helixi376 – 388Combined sources13
Helixi409 – 427Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EPJX-ray1.70A2-429[»]
2ZSLX-ray1.70A2-429[»]
2ZSMX-ray2.30A/B/C2-429[»]
ProteinModelPortaliQ9Y9I9.
SMRiQ9Y9I9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y9I9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG00918. Archaea.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.

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.

Q9Y9I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGEKSRML FERTKELFPG GVNSPVRAAV KPYPFYVKRG EGAYLYTVDG
60 70 80 90 100
ARIVDLVLAY GPLILGHKHP RVLEAVEEAL ARGWLYGAPG EAEVLLAEKI
110 120 130 140 150
LGYVKRGGMI RFVNSGTEAT MTAIRLARGY TGRDLILKFD GCYHGSHDAV
160 170 180 190 200
LVAAGSAAAH YGVPTSAGVP EAVARLTLVT PYNDVEALER VFAEYGDRIA
210 220 230 240 250
GVIVEPVIAN AGVIPPRREF LAALQRLSRE SGALLILDEV VTGFRLGLEG
260 270 280 290 300
AQGYFNIEGD IIVLGKIIGG GFPVGAVAGS REVMSLLTPQ GKVFNAGTFN
310 320 330 340 350
AHPITMAAGL ATLKALEEEP VYSVSREAAK ALEEAASEVL DRTGLPYTIN
360 370 380 390 400
RVESMMQLFI GVEEVSNAAQ ARKADKKFYV KLHEEMLRRG VFIAPSNLEA
410 420
VFTGLPHQGE ALEIAVEGLR SSLKTVLGS
Length:429
Mass (Da):45,954
Last modified:July 10, 2007 - v2
Checksum:i6CC7C5A97EE1F65C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA81311.2.
PIRiG72456.

Genome annotation databases

EnsemblBacteriaiBAA81311; BAA81311; APE_2299.1.
KEGGiape:APE_2299.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000002 Genomic DNA. Translation: BAA81311.2.
PIRiG72456.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EPJX-ray1.70A2-429[»]
2ZSLX-ray1.70A2-429[»]
2ZSMX-ray2.30A/B/C2-429[»]
ProteinModelPortaliQ9Y9I9.
SMRiQ9Y9I9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272557.APE_2299.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA81311; BAA81311; APE_2299.1.
KEGGiape:APE_2299.1.

Phylogenomic databases

eggNOGiarCOG00918. Archaea.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

Miscellaneous databases

EvolutionaryTraceiQ9Y9I9.

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_AERPE
AccessioniPrimary (citable) accession number: Q9Y9I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 10, 2007
Last modified: November 2, 2016
This is version 108 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.