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B1XD24

- GSA_ECODH

UniProt

B1XD24 - GSA_ECODH

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Escherichia coli (strain K12 / DH10B)
Status
Reviewed - 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

BioCyciECOL316385:GJ8B-132-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:ECDH10B_0134
OrganismiEscherichia coli (strain K12 / DH10B)
Taxonomic identifieri316385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001689: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamate-1-semialdehyde 2,1-aminomutasePRO_1000121883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiB1XD24.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi316385.ECDH10B_0134.

Structurei

3D structure databases

ProteinModelPortaliB1XD24.
SMRiB1XD24. Positions 1-426.
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.
OMAiRAIKPYP.
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.

B1XD24-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKSENLYSA ARELIPGGVN SPVRAFTGVG GTPLFIEKAD GAYLYDVDGK
60 70 80 90 100
AYIDYVGSWG PMVLGHNHPA IRNAVIEAAE RGLSFGAPTE MEVKMAQLVT
110 120 130 140 150
ELVPTMDMVR MVNSGTEATM SAIRLARGFT GRDKIIKFEG CYHGHADCLL
160 170 180 190 200
VKAGSGALTL GQPNSPGVPA DFAKYTLTCT YNDLASVRAA FEQYPQEIAC
210 220 230 240 250
IIVEPVAGNM NCVPPLPEFL PGLRALCDEF GALLIIDEVM TGFRVALAGA
260 270 280 290 300
QDYYGVVPDL TCLGKIIGGG MPVGAFGGRR DVMDALAPTG PVYQAGTLSG
310 320 330 340 350
NPIAMAAGFA CLNEVAQPGV HETLDELTTR LAEGLLEAAE EAGIPLVVNH
360 370 380 390 400
VGGMFGIFFT DAESVTCYQD VMACDVERFK RFFHMMLDEG VYLAPSAFEA
410 420
GFMSVAHSME DINNTIDAAR RVFAKL
Length:426
Mass (Da):45,366
Last modified:May 20, 2008 - v1
Checksum:iBED817E100468CF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000948 Genomic DNA. Translation: ACB01333.1.
RefSeqiYP_001729111.1. NC_010473.1.

Genome annotation databases

EnsemblBacteriaiACB01333; ACB01333; ECDH10B_0134.
GeneIDi6062269.
KEGGiecd:ECDH10B_0134.
PATRICi18460020. VBIEscCol59506_0137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000948 Genomic DNA. Translation: ACB01333.1 .
RefSeqi YP_001729111.1. NC_010473.1.

3D structure databases

ProteinModelPortali B1XD24.
SMRi B1XD24. Positions 1-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 316385.ECDH10B_0134.

Proteomic databases

PRIDEi B1XD24.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB01333 ; ACB01333 ; ECDH10B_0134 .
GeneIDi 6062269.
KEGGi ecd:ECDH10B_0134.
PATRICi 18460020. VBIEscCol59506_0137.

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
KOi K01845.
OMAi RAIKPYP.
OrthoDBi EOG6QVRHN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci ECOL316385:GJ8B-132-MONOMER.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPi MF_00375. HemL_aminotrans_3.
InterProi IPR004639. 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 ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR00713. hemL. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
    Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
    J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / DH10B.

Entry informationi

Entry nameiGSA_ECODH
AccessioniPrimary (citable) accession number: B1XD24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: November 26, 2014
This is version 54 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

Documents

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

External Data

Dasty 3