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A6VUX8 (GSA_MARMS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:Mmwyl1_1328
OrganismMarinomonas sp. (strain MWYL1) [Complete proteome] [HAMAP]
Taxonomic identifier400668 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesMarinomonas

Protein attributes

Sequence length427 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 – 427427Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_1000079925

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VUX8 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: D701B9A1BB20BB70

FASTA42745,875
        10         20         30         40         50         60 
MSRSEDLYAR AQHRIPGGVN SPVRAFNGVG GTPIFFQRGE GAYVYDEDKK RYIDYVGSWG 

        70         80         90        100        110        120 
PMILGHSHPD VLDAVRQQLD FGLSFGAPTE VEITMAEKVC ELVPSMDMVR MVNSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT GRDKIVKFEG CYHGHSDSLL VKAGSGALTL GVPNSPGVPA DLAQHTITLQ 

       190        200        210        220        230        240 
YNDIEEVKRC FSEIGDQIAC IIVEPVAGNM NCILPVEGFL ETLRKVCDES GAVLIFDEVM 

       250        260        270        280        290        300 
TGFRVALGGA QAHFGIVPDL TTLGKVIGAG MPVGAFGGKR EIMEHISPLG PVYQAGTLSG 

       310        320        330        340        350        360 
NPVAMVAGLA VLNKISEEGF HQTLGTKADR LVSGLKQAAD EAGVPFCVVS VGGMFGFFFT 

       370        380        390        400        410        420 
EAEVVATFAD VQKCDLSKFK AFFHYMLEEG VYFAPAAFEA GFISQAHTEE DIDYTIEAAK 


RSFAKLV 

« Hide

References

[1]"Complete sequence of Marinomonas sp. MWYL1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MWYL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000749 Genomic DNA. Translation: ABR70257.1.
RefSeqYP_001340192.1. NC_009654.1.

3D structure databases

ProteinModelPortalA6VUX8.
SMRA6VUX8. Positions 2-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400668.Mmwyl1_1328.

Proteomic databases

PRIDEA6VUX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR70257; ABR70257; Mmwyl1_1328.
GeneID5368651.
KEGGmmw:Mmwyl1_1328.
PATRIC22465937. VBIMarSp124341_1369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMACSWGPLI.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycMSP400668:GHKD-1338-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_MARMS
AccessionPrimary (citable) accession number: A6VUX8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 49 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