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C1A7K7 (GSA_GEMAT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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

Short name=GSA
EC=5.4.3.8
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT
Gene names
Name:hemL
Ordered Locus Names:GAU_1175
OrganismGemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC 100505) [Complete proteome] [HAMAP]
Taxonomic identifier379066 [NCBI]
Taxonomic lineageBacteriaGemmatimonadetesGemmatimonadalesGemmatimonadaceaeGemmatimonas

Protein attributes

Sequence length435 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 – 435435Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000382318

Amino acid modifications

Modified residue2691N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1A7K7 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 640DC2F8532A7343

FASTA43545,841
        10         20         30         40         50         60 
MTEMVPHARS AEIMARARMR FPGGVNSPVR AFRGVGGEPF VAARGKGARI WDVDGNEYFD 

        70         80         90        100        110        120 
YVLSWGPLVL GHAPDVVLHA VSQAMLEGTS FGMPTAREVE LADAIAGRMP HLEMVRFTSS 

       130        140        150        160        170        180 
GTEATMSIAR LARAVTKREH ILKFDGCYHG HGDSFLVRAG SGVATLGLPD SPGVPEALAK 

       190        200        210        220        230        240 
LTLTCAFNDL DAVERIARDV PLAAIMLEPI VGNSGFIEPT PGFIQGLRRI ADETGALLVF 

       250        260        270        280        290        300 
DEVMTGFRIA FGGATEYFGV TPDLTALGKV IGGGLPVAAY GGSRTLMEHI APTGPVYQAG 

       310        320        330        340        350        360 
TLSGNPLAMA AGIATLGALT RSVHDEITNQ TAALVDGLRG IATRRGVPLS ARHVGSMWGF 

       370        380        390        400        410        420 
FFRDGDVHSF DDAKQSDVAL FRRFFHAART RGVSLAPSAF EAAFMSAAHG PAEVGETLSR 

       430 
LDDALGAALT DTAGH 

« Hide

References

[1]"Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a novel phylum Gemmatimonadetes."
Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A., Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H., Tanikawa S., Hanada S., Kamagata Y., Fujita N.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T-27 / DSM 14586 / JCM 11422 / NBRC 100505.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009153 Genomic DNA. Translation: BAH38217.1.
RefSeqYP_002760687.1. NC_012489.1.

3D structure databases

ProteinModelPortalC1A7K7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING379066.GAU_1175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH38217; BAH38217; GAU_1175.
GeneID7705303.
KEGGgau:GAU_1175.
PATRIC21955192. VBIGemAur55831_1210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycGAUR379066:GI3W-1188-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.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGSA_GEMAT
AccessionPrimary (citable) accession number: C1A7K7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 36 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