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Protein

Glutamate-1-semialdehyde 2,1-aminomutase 2

Gene

hemL2

Organism
Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
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

BioCyciBBRE358681:GHYS-1919-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:BBR47_18060
OrganismiBrevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
Taxonomic identifieri358681 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus
ProteomesiUP000001877: 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 – 429429Glutamate-1-semialdehyde 2,1-aminomutase 2PRO_0000382285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiC0ZAH4.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi358681.BBR47_18060.

Structurei

3D structure databases

ProteinModelPortaliC0ZAH4.
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]
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.

C0ZAH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNREKSTQLF AEAQHYIPGG VNSPVRAFKS VGGNPVYIEK GEGSRIFDVD
60 70 80 90 100
GNSYIDYIGS WGPLILGHAH PRVLAAITEV AALGTSFGAP TERETEMAKL
110 120 130 140 150
VCEIVPSVEV VRMVNSGTEA TMSALRLARG YTRRNKIMKF EGCYHGHADS
160 170 180 190 200
LLIKAGSGVA TLGLPDSPGV PEGTAHNTIT VPYNDLESVK LAFEAFGDDL
210 220 230 240 250
AAVIVEPIGG NMGVVPPQPG FLEGLREITE KHGTLLIFDE VMTGFRVALG
260 270 280 290 300
GAQELYGITP DLTTMGKVIG GGLPVGAYGG KREIMQQVAP AGPIYQAGTL
310 320 330 340 350
SGNPLAMAAG LTTLQELSKP GAYERLEKMS ARLAEGLADN AKKLGIPHTL
360 370 380 390 400
NRVGSMVCLF FTETPVINYE TAKTSDLERF SAYFSYLLEE GVMIPPSQFE
410 420
GMFVSLAHTD EDIERTIEAS YQAMKKAFK
Length:429
Mass (Da):45,955
Last modified:May 26, 2009 - v1
Checksum:i77DF96DC90C532F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008955 Genomic DNA. Translation: BAH42783.1.
RefSeqiYP_002771287.1. NC_012491.1.

Genome annotation databases

EnsemblBacteriaiBAH42783; BAH42783; BBR47_18060.
GeneIDi7719682.
KEGGibbe:BBR47_18060.
PATRICi21233920. VBIBreBre96763_1794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008955 Genomic DNA. Translation: BAH42783.1.
RefSeqiYP_002771287.1. NC_012491.1.

3D structure databases

ProteinModelPortaliC0ZAH4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi358681.BBR47_18060.

Proteomic databases

PRIDEiC0ZAH4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAH42783; BAH42783; BBR47_18060.
GeneIDi7719682.
KEGGibbe:BBR47_18060.
PATRICi21233920. VBIBreBre96763_1794.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciBBRE358681:GHYS-1919-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. "Brevibacillus brevis strain 47, complete genome."
    Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W., Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S., Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.
    , Udaka S., Tanikawa S., Fujita N.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 47 / JCM 6285 / NBRC 100599.

Entry informationi

Entry nameiGSA2_BREBN
AccessioniPrimary (citable) accession number: C0ZAH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: March 4, 2015
This is version 46 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.