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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Clostridium kluyveri (strain NBRC 12016)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi

GO - Molecular functioni

  1. glutamate-1-semialdehyde 2,1-aminomutase activity Source: UniProtKB-HAMAP
  2. pyridoxal phosphate binding Source: InterPro
  3. transaminase activity Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciCKLU583346:GJNQ-617-MONOMER.
UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation (EC:5.4.3.8UniRule annotation)
Short name:
GSAUniRule annotation
Alternative name(s):
Glutamate-1-semialdehyde aminotransferaseUniRule annotation
Short name:
GSA-ATUniRule annotation
Gene namesi
Name:hemLUniRule annotation
Ordered Locus Names:CKR_0584
OrganismiClostridium kluyveri (strain NBRC 12016)
Taxonomic identifieri583346 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000007969 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei264 – 2641N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi583346.CKR_0584.

Structurei

3D structure databases

ProteinModelPortaliB9DZG0.
SMRiB9DZG0. Positions 3-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OrthoDBiEOG6QVRHN.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 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]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B9DZG0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNDKIFEES KLYMPGGVNS PVRAFKDVPL NPPVIKKGRG AYIYDEDGNE
60 70 80 90 100
YIDFVCSWGP MILGHCDEDV VNAIKYTSEN AISFGATTKI ELELSKYICT
110 120 130 140 150
TMDNIEMIRM VNSGTEATMS AVKLARGYTR RNKIIKFSGC YHGHFDDFLV
160 170 180 190 200
EAGSGVMTEG IPGSAGVPKD SIKNTIIAEY NNLEDVKNIF NKYGSDTAAI
210 220 230 240 250
IVEPVAGNMG VIPGRIDFLK GLRKLCDEYG SLLIFDEVMS GFRVAYKGAQ
260 270 280 290 300
SLYGIKPDIT TMAKIMGGGL PCGAYGGRKD IMENLSPLGP VYQAGTMSGN
310 320 330 340 350
PIVMAAGLAT LKKLNENPDY YVKLEKLGKK LEKGIKQISK DKNIPMVINR
360 370 380 390 400
CGAMFSIFFT SDSEVKNYKD ARKCDTTIFA KFFQHMLERG IYIAPSQFEA
410 420
IFLNVKHTEE HIDKFLQAVN TF
Length:422
Mass (Da):46,726
Last modified:September 1, 2009 - v2
Checksum:iFAEAEDE075C78EA7
GO

Sequence cautioni

The sequence BAH05635.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009049 Genomic DNA. Translation: BAH05635.1. Different initiation.
RefSeqiYP_002471049.1. NC_011837.1.

Genome annotation databases

EnsemblBacteriaiBAH05635; BAH05635; CKR_0584.
KEGGickr:CKR_0584.
PATRICi19470918. VBICloKlu118830_0718.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009049 Genomic DNA. Translation: BAH05635.1. Different initiation.
RefSeqiYP_002471049.1. NC_011837.1.

3D structure databases

ProteinModelPortaliB9DZG0.
SMRiB9DZG0. Positions 3-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi583346.CKR_0584.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAH05635; BAH05635; CKR_0584.
KEGGickr:CKR_0584.
PATRICi19470918. VBICloKlu118830_0718.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciCKLU583346:GJNQ-617-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3.
InterProiIPR004639. 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]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of Clostridium kluyveri and comparative genomics of Clostridia species."
    Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A., Yukawa H.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NBRC 12016.

Entry informationi

Entry nameiGSA_CLOK1
AccessioniPrimary (citable) accession number: B9DZG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: September 1, 2009
Last modified: April 1, 2015
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.