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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Bacillus subtilis (strain 168)
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 2 (gsaB), 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

BioCyciBSUB:BSU28120-MONOMER.
BRENDAi5.4.3.8. 658.
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
Synonyms:hemK
Ordered Locus Names:BSU28120
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001203931 – 430Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei268N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

PaxDbiP30949.
PRIDEiP30949.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015366.

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 15Combined sources11
Helixi19 – 21Combined sources3
Beta strandi22 – 24Combined sources3
Helixi25 – 28Combined sources4
Turni30 – 33Combined sources4
Beta strandi39 – 44Combined sources6
Beta strandi46 – 49Combined sources4
Beta strandi54 – 59Combined sources6
Helixi60 – 62Combined sources3
Helixi72 – 84Combined sources13
Helixi93 – 105Combined sources13
Beta strandi110 – 116Combined sources7
Helixi118 – 133Combined sources16
Beta strandi137 – 142Combined sources6
Helixi150 – 152Combined sources3
Beta strandi158 – 161Combined sources4
Beta strandi165 – 168Combined sources4
Beta strandi179 – 183Combined sources5
Helixi187 – 197Combined sources11
Helixi198 – 200Combined sources3
Beta strandi201 – 206Combined sources6
Beta strandi208 – 210Combined sources3
Beta strandi212 – 214Combined sources3
Helixi222 – 233Combined sources12
Beta strandi236 – 240Combined sources5
Turni242 – 247Combined sources6
Helixi252 – 256Combined sources5
Beta strandi262 – 266Combined sources5
Helixi268 – 271Combined sources4
Beta strandi277 – 281Combined sources5
Helixi283 – 286Combined sources4
Turni290 – 292Combined sources3
Beta strandi293 – 295Combined sources3
Helixi305 – 316Combined sources12
Helixi320 – 343Combined sources24
Beta strandi349 – 353Combined sources5
Beta strandi356 – 364Combined sources9
Helixi369 – 372Combined sources4
Helixi377 – 389Combined sources13
Beta strandi396 – 400Combined sources5
Helixi410 – 429Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BS8X-ray2.30A1-430[»]
ProteinModelPortaliP30949.
SMRiP30949.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30949.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiP30949.
KOiK01845.
OMAiCGHAHPE.
PhylomeDBiP30949.

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.

P30949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSYEKSKTA FKEAQKLMPG GVNSPVRAFK SVDMDPIFME RGKGSKIFDI
60 70 80 90 100
DGNEYIDYVL SWGPLILGHT NDRVVESLKK VAEYGTSFGA PTEVENELAK
110 120 130 140 150
LVIDRVPSVE IVRMVSSGTE ATMSALRLAR GYTGRNKILK FEGCYHGHGD
160 170 180 190 200
SLLIKAGSGV ATLGLPDSPG VPEGIAKNTI TVPYNDLESV KLAFQQFGED
210 220 230 240 250
IAGVIVEPVA GNMGVVPPQE GFLQGLRDIT EQYGSLLIFD EVMTGFRVDY
260 270 280 290 300
NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKAEIMEQIA PSGPIYQAGT
310 320 330 340 350
LSGNPLAMTA GLETLKQLTP ESYKNFIKKG DRLEEGISKT AGAHGIPHTF
360 370 380 390 400
NRAGSMIGFF FTNEPVINYE TAKSSDLKLF ASYYKGMANE GVFLPPSQFE
410 420 430
GLFLSTAHTD EDIENTIQAA EKVFAEISRR
Length:430
Mass (Da):46,449
Last modified:July 1, 1993 - v1
Checksum:iFBC7CF1784C46017
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57676 Genomic DNA. Translation: AAA22515.1.
AL009126 Genomic DNA. Translation: CAB14772.1.
PIRiD42728.
RefSeqiNP_390690.1. NC_000964.3.
WP_004398699.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14772; CAB14772; BSU28120.
GeneIDi937490.
KEGGibsu:BSU28120.
PATRICi18977500. VBIBacSub10457_2939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57676 Genomic DNA. Translation: AAA22515.1.
AL009126 Genomic DNA. Translation: CAB14772.1.
PIRiD42728.
RefSeqiNP_390690.1. NC_000964.3.
WP_004398699.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BS8X-ray2.30A1-430[»]
ProteinModelPortaliP30949.
SMRiP30949.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015366.

Proteomic databases

PaxDbiP30949.
PRIDEiP30949.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14772; CAB14772; BSU28120.
GeneIDi937490.
KEGGibsu:BSU28120.
PATRICi18977500. VBIBacSub10457_2939.

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
InParanoidiP30949.
KOiK01845.
OMAiCGHAHPE.
PhylomeDBiP30949.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBSUB:BSU28120-MONOMER.
BRENDAi5.4.3.8. 658.

Miscellaneous databases

EvolutionaryTraceiP30949.

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_BACSU
AccessioniPrimary (citable) accession number: P30949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 2016
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.