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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923)
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

BioCyciDDES546414:GHOM-1810-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:Deide_15910
OrganismiDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923)
Taxonomic identifieri546414 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002208 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 – 441441Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PaxDbiC1CWI8.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi546414.Deide_15910.

Structurei

3D structure databases

ProteinModelPortaliC1CWI8.
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.
OMAiCGHAHPE.
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.

C1CWI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSTTTRSE ALFERARAVT PGGVNSPVRA FKSVGGVPRF IREAHGAYLT
60 70 80 90 100
DMDDTRYVDY IGSWGPMILG HDHPTIREAI ATALTGGTSF GAPGEREVEL
110 120 130 140 150
AELVTRLTGA GRVRFVNSGT EATMSALRLA RGFTGRKFIV KFRGNYHGHA
160 170 180 190 200
DGLLVEAGSG LLTNAEGVLG SAAPSSAGVP EEYASLTLVS EYNDPAALDA
210 220 230 240 250
LMRLRGHEVA AVIFEPVVGN AGVLVPTPDF LEALHRVKAS GALLVADEVM
260 270 280 290 300
TGFRLSLNGA TGLLGLEPDL TCWGKIIGGG LPVGAYGGRA DVMDFVSPQG
310 320 330 340 350
PVYQAGTLSG NPLAMAAGLA TLQTLEADPG IYGRLEAYTA ALASGLRAAA
360 370 380 390 400
DEAGVPVSIN RVGSMLTAFH QDVPDGSIRT YADAARSDTT GFATWFQGML
410 420 430 440
ARGVYWAPSQ FESIFVSGAH TDRELNVTLE AARSAYGGTP V
Length:441
Mass (Da):46,023
Last modified:May 26, 2009 - v1
Checksum:i9C8DFC10F064CD60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001114 Genomic DNA. Translation: ACO46555.1.
RefSeqiWP_012693678.1. NC_012526.1.
YP_002786309.1. NC_012526.1.

Genome annotation databases

EnsemblBacteriaiACO46555; ACO46555; Deide_15910.
KEGGiddr:Deide_15910.
PATRICi21617108. VBIDeiDes121019_1832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001114 Genomic DNA. Translation: ACO46555.1.
RefSeqiWP_012693678.1. NC_012526.1.
YP_002786309.1. NC_012526.1.

3D structure databases

ProteinModelPortaliC1CWI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi546414.Deide_15910.

Proteomic databases

PaxDbiC1CWI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACO46555; ACO46555; Deide_15910.
KEGGiddr:Deide_15910.
PATRICi21617108. VBIDeiDes121019_1832.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciDDES546414:GHOM-1810-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VCD115 / DSM 17065 / LMG 22923.

Entry informationi

Entry nameiGSA_DEIDV
AccessioniPrimary (citable) accession number: C1CWI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: May 26, 2009
Last modified: April 1, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference 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.