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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
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. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciCTHA517418:GHTO-25-MONOMER.
UniPathwayiUPA00251; UER00317.
UPA00668.

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:Ctha_0025
OrganismiChloroherpeton thalassium (strain ATCC 35110 / GB-78)
Taxonomic identifieri517418 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChloroherpeton
ProteomesiUP000001208: 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 – 432432Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000121868Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiB3QSA6.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi517418.Ctha_0025.

Structurei

3D structure databases

ProteinModelPortaliB3QSA6.
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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B3QSA6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNLKTSAAL FERAKKVIPG GVNSPVRAFN SVGGTPVFVT KGEGARMIDV
60 70 80 90 100
DGNSYIDYVG SWGPFILGHS HPRVIEAIER TMKAHGTSFG APTELEIELA
110 120 130 140 150
ELIIKVVPSV EMVRMVNSGT EATMSAIRLA RGYTKREKII KFEGCYHGHG
160 170 180 190 200
DSFLIKAGSG ALTLGAPSSP GVTEGTAKDT LNATYNDIES VRALVDSNKG
210 220 230 240 250
NVAAIIIEAV GGNMGVVPSK KEFLVALREL CDKEGIVLIF DEVMTGFRVA
260 270 280 290 300
LGGAQEVYGI TPDLTTMGKI IGGGLPVGAY GGKKEIMEHV SPVGTVYQAG
310 320 330 340 350
TLSGNPLAMS AGLATIKILA EENPYPELEK KAVIIEEGFK SNLEKLGLNL
360 370 380 390 400
CQTRVGSMSC LFFTDKEVVD FETANSSDTA KFATYFNSML ESGIYLACSQ
410 420 430
FEAMFISTMH TEEDLQKTIE ANYNALKLAY GK
Length:432
Mass (Da):46,182
Last modified:September 2, 2008 - v1
Checksum:iD2E8996B075EFDB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001100 Genomic DNA. Translation: ACF12497.1.
RefSeqiYP_001994944.1. NC_011026.1.

Genome annotation databases

EnsemblBacteriaiACF12497; ACF12497; Ctha_0025.
GeneIDi6421197.
KEGGicts:Ctha_0025.
PATRICi21428401. VBIChlTha99257_0031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001100 Genomic DNA. Translation: ACF12497.1.
RefSeqiYP_001994944.1. NC_011026.1.

3D structure databases

ProteinModelPortaliB3QSA6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi517418.Ctha_0025.

Proteomic databases

PRIDEiB3QSA6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACF12497; ACF12497; Ctha_0025.
GeneIDi6421197.
KEGGicts:Ctha_0025.
PATRICi21428401. VBIChlTha99257_0031.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciCTHA517418:GHTO-25-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]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Chloroherpeton thalassium ATCC 35110."
    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., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35110 / GB-78.

Entry informationi

Entry nameiGSA_CHLT3
AccessioniPrimary (citable) accession number: B3QSA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: February 4, 2015
This is version 53 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.