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Q2Y5Q5 (GSA_NITMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:Nmul_A2629
OrganismNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849) [Complete proteome] [HAMAP]
Taxonomic identifier323848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira

Protein attributes

Sequence length425 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 – 425425Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375
PRO_0000243589

Amino acid modifications

Modified residue2651N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2Y5Q5 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: CFD85461E5F0199C

FASTA42544,870
        10         20         30         40         50         60 
MSRNQQLFEQ SQKFIPGGVN SPVRAFKSVG GTPVFFRKGE GAYAWDADDK SYIDYVGSWG 

        70         80         90        100        110        120 
PLILGHAHPE VVDAVYAAAK NGLTFGAPTE AELEIAELLC RLVPSIEQVR LVSSGTEATM 

       130        140        150        160        170        180 
SAIRLARGYT ARNRIIKFEG CYHGHDDALL VKAGSGALTF GHPSSAGVPV ETASSTVVLD 

       190        200        210        220        230        240 
YNDLAGVEQA FNQFGAEIAA VIVEPVAGNM NLIAPQPGFL AGLRELCTRH GSVLIFDEVM 

       250        260        270        280        290        300 
TGFRVGLECA QGLYGIKPDL TTLGKVIGGG MPMAAFGGRR EIMQCLAPVG AVYQAGTLSG 

       310        320        330        340        350        360 
NPVAVAAGLA TLKLVQVPGF YDKLAARTRK LTEGLAAAAA KQGVVFCAEA VGGMFGLYFR 

       370        380        390        400        410        420 
ESAPKSYAEV MSCDREAFNG FFHAMLEEGI YFAPSAFEAG FVSAAHGDAE ISKTLATAEK 


IFARE 

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References

[1]"Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25196 / NCIMB 11849.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000103 Genomic DNA. Translation: ABB75916.1.
RefSeqYP_413308.1. NC_007614.1.

3D structure databases

ProteinModelPortalQ2Y5Q5.
SMRQ2Y5Q5. Positions 3-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323848.Nmul_A2629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB75916; ABB75916; Nmul_A2629.
GeneID3786332.
KEGGnmu:Nmul_A2629.
PATRIC22729008. VBINitMul110821_3052.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0001.
HOGENOMHOG000020210.
KOK01845.
OMARAIKPYP.
OrthoDBEOG6QVRHN.

Enzyme and pathway databases

BioCycNMUL323848:GKEC-2675-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_NITMU
AccessionPrimary (citable) accession number: Q2Y5Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 66 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