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B4UKE6 (GSA_ANASK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:AnaeK_4480
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length430 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 – 430430Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000121856

Amino acid modifications

Modified residue2671N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B4UKE6 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 7E623CCCB93C3A12

FASTA43045,472
        10         20         30         40         50         60 
MKTELSQKLF EKANDLFPGG VNSPVRAFKG VGGTPRFISR AKGSHIFDVD GNDYVDYVLS 

        70         80         90        100        110        120 
WGPMIVGHCH PEVMREVQDA MKEGSSFGAP SPREILLAEL VRERMPWVEK MRFVSSGTEA 

       130        140        150        160        170        180 
TTSAIRVARG FTGRDDIVKF DGCYHGAGDP LLVKAGSGVE TLGLPDSPGV PADVARHTLT 

       190        200        210        220        230        240 
APYNDLPALE QVFQAKGASI AAVILEPVVG NMGVLVPRPG FLQGVHDLCR KHGALFIVDE 

       250        260        270        280        290        300 
VMTGFRLSSG GACGLYGLRP DLVTFGKVIG AGLPVGAFGG RRDVMDRVAP AGPIYQAGTL 

       310        320        330        340        350        360 
SGNPMAMAAG HAALKLMTEA AYRKLEALSA ALAEGLQAAA AEAKVPVQVN RVGSMLTVFF 

       370        380        390        400        410        420 
SDRPVFDAAS ARACNTRRFG AFFHAMLEHG AYLPPSQFEA AFLSTAHTDD DVARTVAAAR 

       430 
LAFAEAAKVA 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter sp. K."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001131 Genomic DNA. Translation: ACG75682.1.
RefSeqYP_002136811.1. NC_011145.1.

3D structure databases

ProteinModelPortalB4UKE6.
SMRB4UKE6. Positions 1-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING447217.AnaeK_4480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG75682; ACG75682; AnaeK_4480.
GeneID6784495.
KEGGank:AnaeK_4480.
PATRIC20943644. VBIAnaSp90767_4488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARFMVSGN.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycASP447217:GHB0-4539-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_ANASK
AccessionPrimary (citable) accession number: B4UKE6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 45 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