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C0Z671 (GSA1_BREBN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate-1-semialdehyde 2,1-aminomutase 1

Short name=GSA 1
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase 1
Short name=GSA-AT 1
Gene names
Name:hemL1
Ordered Locus Names:BBR47_10510
OrganismBrevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599) [Complete proteome] [HAMAP]
Taxonomic identifier358681 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00375

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00375

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00375.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

transaminase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 428428Glutamate-1-semialdehyde 2,1-aminomutase 1 HAMAP-Rule MF_00375
PRO_0000382284

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C0Z671 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 4FAECA7240D6C951

FASTA42845,873
        10         20         30         40         50         60 
MKRERSAQLH EQALDVILGG VNSPSRSFKA VGGGAPVTME RAQGAYFWDV DGNRYIDYLA 

        70         80         90        100        110        120 
AYGPIITGHA HPHVTNAICE AATNGTLYGT PTPWEITFAN MIREAIPSME RIRFNNSGTE 

       130        140        150        160        170        180 
AVMTCIRVAR AYTGRVKIIK FAGCYHGHSD LVLVAAGSGP STLGIPDSAG IPQSIASEVI 

       190        200        210        220        230        240 
TVPFNNIEAF AEAMSKWGSE TACVLVEPIV GNFGIVAPEP GFLEEVNRIT HEAGALVVYD 

       250        260        270        280        290        300 
EVITAFRFCY GGAQNLLGVE PDLTALGKII GGGLPIGAYG GRREIMEQVA PLGPAYQAGT 

       310        320        330        340        350        360 
MAGNPASIRA GIACLEVLKQ PSVYDEFERL GARLANGIIE AANKHGVTIQ LNRVKGALAV 

       370        380        390        400        410        420 
YFTDEPVHDY DAAQKANGEV FARFFQLMLN EGVCLAPSKY EAWFVTTAHT EEDIQFTIAA 


VDRAFSQL 

« Hide

References

[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008955 Genomic DNA. Translation: BAH42028.1.
RefSeqYP_002770532.1. NC_012491.1.

3D structure databases

ProteinModelPortalC0Z671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING358681.BBR47_10510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH42028; BAH42028; BBR47_10510.
GeneID7718256.
KEGGbbe:BBR47_10510.
PATRIC21232388. VBIBreBre96763_1045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMAFNDIDSY.
OrthoDBEOG6QVRHN.
ProtClustDBPRK12389.

Enzyme and pathway databases

BioCycBBRE358681:GHYS-1147-MONOMER.
UniPathwayUPA00251; UER00317.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_00375. HemL_aminotrans_3.
InterProIPR004639. 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]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00713. hemL. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGSA1_BREBN
AccessionPrimary (citable) accession number: C0Z671
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways