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 1

Gene

hemL1

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
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

BioCyciBHAL272558:GJC5-1001-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1UniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSA 1UniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1UniRule annotation
Short name:
GSA-AT 1UniRule annotation
Gene namesi
Name:hemL1UniRule annotation
Synonyms:gsaB
Ordered Locus Names:BH0943
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: 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 – 437437Glutamate-1-semialdehyde 2,1-aminomutase 1PRO_0000120394Add
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

STRINGi272558.BH0943.

Structurei

3D structure databases

ProteinModelPortaliQ9KEB0.
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.
OMAiEMFAKFF.
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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KEB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRSRSESLF QKAQSLIVGG VNSPSRSFKA VGGGAPVFME KAKGAYFWDV
60 70 80 90 100
DGNQYIDYLA AYGPIITGHA HPHITNAIQR AAENGVLYGT PTKLENQFAS
110 120 130 140 150
MLQQAIPSLE KVRFVNSGTE AVMTTIRVAR AYTGRDKIIK FAGCYHGHSD
160 170 180 190 200
LVLVAAGSGP STLGTPDSAG VTKNIAEEVI TVPFNQLDSL KEALDHWGEE
210 220 230 240 250
VAAVLVEPIV GNFGIVEPHE GFLEGVNELA HNAGALVIYD EVITAFRFMY
260 270 280 290 300
EGAQNYVGVE PDMTALGKII GGGLPIGAYG GRIDIMEKVA PLGPAYQAGT
310 320 330 340 350
MAGNPASMSA GIACLEVLQE EGLYDELDRK GAILEKGIKA HAEAHGITIS
360 370 380 390 400
INRLKGALTV YFTDETVTCY EQAERSDGEK FSLFFKEMLN QGINLAPSKY
410 420 430
EAWFLTIAHT DEDIEKTLQA VDHAFSVMAA KGYHLKR
Length:437
Mass (Da):47,080
Last modified:October 1, 2000 - v1
Checksum:iF2035E49347BE0A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04662.1.
PIRiG83767.
RefSeqiNP_241809.1. NC_002570.2.
WP_010897115.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB04662; BAB04662; BAB04662.
GeneIDi893889.
KEGGibha:BH0943.
PATRICi18938906. VBIBacHal18977_0991.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA. Translation: BAB04662.1.
PIRiG83767.
RefSeqiNP_241809.1. NC_002570.2.
WP_010897115.1. NC_002570.2.

3D structure databases

ProteinModelPortaliQ9KEB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272558.BH0943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB04662; BAB04662; BAB04662.
GeneIDi893889.
KEGGibha:BH0943.
PATRICi18938906. VBIBacHal18977_0991.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiEMFAKFF.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBHAL272558:GJC5-1001-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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Entry informationi

Entry nameiGSA1_BACHD
AccessioniPrimary (citable) accession number: Q9KEB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 102 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.