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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Bacillus licheniformis (strain DSM 13 / ATCC 14580)
Status
Reviewed-Annotation score: Annotation score: 3 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

BioCyciBLIC279010:GJ2P-2919-MONOMER.
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:BLi02942, BL00628
OrganismiBacillus licheniformis (strain DSM 13 / ATCC 14580)
Taxonomic identifieri279010 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000000608 Componenti: Chromosome UP000000606 Componenti: Chromosome

Subcellular locationi

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 – 431431Glutamate-1-semialdehyde 2,1-aminomutase 2PRO_0000243547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi279010.BL00628.

Structurei

3D structure databases

ProteinModelPortaliQ65GK4.
SMRiQ65GK4. Positions 5-423.
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.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

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.

Q65GK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSYEKSKAA FEEAQRVMPG GVNSPVRAFK SVNMDPIFME RGKGSKIYDI
60 70 80 90 100
DGNEYIDYVL SWGPLILGHS NEKVVKEIQK AAEHGTSFGA PTELETELAE
110 120 130 140 150
LVIDRVPSIE IVRMVSSGTE ATMSALRLAR GYTGRNKIVK FEGCYHGHGD
160 170 180 190 200
SLLIKAGSGV ATLGLPDSPG VPESIAKNTI TVPYNDLESM KLVFQEFGDD
210 220 230 240 250
IAGVIVEPVA GNMGVVPPVK GFLEGLRELT ETHGALLIFD EVMTGFRVDY
260 270 280 290 300
NCAQGYFGVT PDLTCLGKVI GGGLPVGAYG GKAEIMEKIA PSGPIYQAGT
310 320 330 340 350
LSGNPLAMTA GLETLKQLTP ESYREFSRKA DRLEKGISEA AEKNGIPCTF
360 370 380 390 400
NRAGSMIGFF FTNGPVINYD TAKQSDLGLF AEYYKGMADE GVFLPPSQFE
410 420 430
GLFLSTAHTD DDIEHTIKAA ERVFERISRS R
Length:431
Mass (Da):46,640
Last modified:October 24, 2004 - v1
Checksum:i124FA66C6C1ED8A1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU41810.1.
CP000002 Genomic DNA. Translation: AAU24448.1.
RefSeqiYP_006714280.1. NC_006322.1.
YP_080086.1. NC_006270.3.

Genome annotation databases

EnsemblBacteriaiAAU24448; AAU24448; BL00628.
AAU41810; AAU41810; BLi02942.
KEGGibld:BLi02942.
bli:BL00628.
PATRICi18951604. VBIBacLic203714_3003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017333 Genomic DNA. Translation: AAU41810.1.
CP000002 Genomic DNA. Translation: AAU24448.1.
RefSeqiYP_006714280.1. NC_006322.1.
YP_080086.1. NC_006270.3.

3D structure databases

ProteinModelPortaliQ65GK4.
SMRiQ65GK4. Positions 5-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279010.BL00628.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAU24448; AAU24448; BL00628.
AAU41810; AAU41810; BLi02942.
KEGGibld:BLi02942.
bli:BL00628.
PATRICi18951604. VBIBacLic203714_3003.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBLIC279010:GJ2P-2919-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. "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
    Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 7:204-211(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13 / ATCC 14580.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13 / ATCC 14580.

Entry informationi

Entry nameiGSA2_BACLD
AccessioniPrimary (citable) accession number: Q65GK4
Secondary accession number(s): Q62S12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2006
Last sequence update: October 24, 2004
Last modified: March 31, 2015
This is version 84 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.