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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Bacillus anthracis
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.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), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL1), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase 2 (hemL2), Glutamate-1-semialdehyde 2,1-aminomutase 1 (hemL1), Glutamate-1-semialdehyde 2,1-aminomutase (hemL2), 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 2UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 2UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 2UniRule annotation
Short name:
GSA-AT 2UniRule annotation
Gene namesi
Name:hemL2UniRule annotation
Ordered Locus Names:BA_4693, GBAA_4693, BAS4358
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

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_00002435371 – 429Glutamate-1-semialdehyde 2,1-aminomutase 2Add BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei268N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ81LD0. 22 interactors.
STRINGi198094.BA_4693.

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 – 28Combined sources4
Helixi30 – 32Combined sources3
Beta strandi39 – 44Combined sources6
Beta strandi46 – 49Combined sources4
Beta strandi54 – 58Combined sources5
Helixi60 – 62Combined sources3
Helixi72 – 84Combined sources13
Helixi93 – 105Combined sources13
Beta strandi110 – 117Combined sources8
Helixi118 – 133Combined sources16
Beta strandi137 – 142Combined sources6
Helixi150 – 152Combined sources3
Helixi173 – 176Combined sources4
Beta strandi179 – 183Combined sources5
Helixi187 – 197Combined sources11
Helixi198 – 200Combined sources3
Beta strandi201 – 206Combined sources6
Beta strandi208 – 210Combined sources3
Helixi222 – 233Combined sources12
Beta strandi236 – 240Combined sources5
Turni242 – 247Combined sources6
Helixi252 – 257Combined sources6
Beta strandi262 – 266Combined sources5
Helixi268 – 271Combined sources4
Beta strandi277 – 281Combined sources5
Helixi283 – 286Combined sources4
Turni290 – 292Combined sources3
Beta strandi293 – 295Combined sources3
Turni300 – 303Combined sources4
Helixi305 – 316Combined sources12
Helixi320 – 343Combined sources24
Beta strandi349 – 353Combined sources5
Beta strandi356 – 364Combined sources9
Helixi369 – 372Combined sources4
Helixi377 – 389Combined sources13
Helixi410 – 425Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K28X-ray1.95A/B/C/D1-429[»]
ProteinModelPortaliQ81LD0.
SMRiQ81LD0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ81LD0.

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.
KOiK01845.
OMAiCGHAHPE.

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.

Q81LD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFDKSIAA FEEAQDLMPG GVNSPVRAFK SVGMNPLFME RGKGSKVYDI
60 70 80 90 100
DGNEYIDYVL SWGPLIHGHA NDRVVEALKA VAERGTSFGA PTEIENKLAK
110 120 130 140 150
LVIERVPSIE IVRMVNSGTE ATMSALRLAR GYTGRNKILK FIGCYHGHGD
160 170 180 190 200
SLLIKAGSGV ATLGLPDSPG VPEGVAKNTI TVAYNDLESV KYAFEQFGDD
210 220 230 240 250
IACVIVEPVA GNMGVVPPQP GFLEGLREVT EQNGALLIFD EVMTGFRVAY
260 270 280 290 300
NCGQGYYGVT PDLTCLGKVI GGGLPVGAYG GKAEIMRQVA PSGPIYQAGT
310 320 330 340 350
LSGNPLAMAA GYETLVQLTP ESYVEFERKA EMLEAGLRKA AEKHGIPHHI
360 370 380 390 400
NRAGSMIGIF FTDEPVINYD AAKSSNLQFF AAYYREMVEQ GVFLPPSQFE
410 420
GLFLSTVHSD ADIEATIAAA EIAMSKLKA
Length:429
Mass (Da):46,060
Last modified:June 1, 2003 - v1
Checksum:i9E56295469536AD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28392.1.
AE017225 Genomic DNA. Translation: AAT56656.1.
AE017334 Genomic DNA. Translation: AAT33816.1.
RefSeqiNP_846906.1. NC_003997.3.
WP_001224513.1. NZ_LHUO01000006.1.
YP_030605.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP28392; AAP28392; BA_4693.
AAT33816; AAT33816; GBAA_4693.
AAT56656; AAT56656; BAS4358.
GeneIDi1083709.
2850472.
KEGGiban:BA_4693.
bar:GBAA_4693.
bat:BAS4358.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP28392.1.
AE017225 Genomic DNA. Translation: AAT56656.1.
AE017334 Genomic DNA. Translation: AAT33816.1.
RefSeqiNP_846906.1. NC_003997.3.
WP_001224513.1. NZ_LHUO01000006.1.
YP_030605.1. NC_005945.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K28X-ray1.95A/B/C/D1-429[»]
ProteinModelPortaliQ81LD0.
SMRiQ81LD0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ81LD0. 22 interactors.
STRINGi198094.BA_4693.

Protocols and materials databases

DNASUi1083709.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP28392; AAP28392; BA_4693.
AAT33816; AAT33816; GBAA_4693.
AAT56656; AAT56656; BAS4358.
GeneIDi1083709.
2850472.
KEGGiban:BA_4693.
bar:GBAA_4693.
bat:BAS4358.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.

Miscellaneous databases

EvolutionaryTraceiQ81LD0.

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 nameiGSA2_BACAN
AccessioniPrimary (citable) accession number: Q81LD0
Secondary accession number(s): Q6HST3, Q6KM26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 105 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. 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.