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P0C2D9

- GSA_CLOPE

UniProt

P0C2D9 - GSA_CLOPE

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Clostridium perfringens (strain 13 / Type A)
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

BioCyciCPER195102:GJFM-1478-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:CPE1432
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000000818: 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 – 425425Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120402Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi195102.CPE1432.

Structurei

3D structure databases

ProteinModelPortaliP0C2D9.
SMRiP0C2D9. Positions 3-422.
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.
OMAiLMAHIAP.
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.

P0C2D9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDRNKEIFEE SKKYMPGGVN SPVRSFGSVG INPPVIKSGK GAMIKDENGN
60 70 80 90 100
EYIDFVLAWG PMILGHCDED VVEAIKKTSE ESIAFGASTK LELDLAKLLC
110 120 130 140 150
ETLDNVDMIR MVNSGTEATM SAVKLARGYT KKDKIIKFAG CYHGHFDGFL
160 170 180 190 200
IEAGSGVLTE GIPGCLGVPE ESIKNTLIGI YNDEKQVEEL FEKYGNDIAG
210 220 230 240 250
IIIEPVAGNM GVVKCDPKFM RKLRELCDKY GALLIFDEVM CGFRVAYKGA
260 270 280 290 300
QTLFDVKPDL VTYAKIMGGG LPCGAYGGRR EIMENLSPLG GVYQAGTMSG
310 320 330 340 350
NPIVMSAGLA TVKKLYENPS YYNHIEKIGS KLEKGVLEIA KKKGLGLVVN
360 370 380 390 400
RQGGMITLFF TDLKEVKCYD DVKTCDGERF KRYFLHMLNK GFNIPPSQFE
410 420
AMFLSVKHTE EHIDKFLEAF ETFEG
Length:425
Mass (Da):46,881
Last modified:January 23, 2007 - v1
Checksum:iB23DFD62CE39B9E2
GO

Sequence cautioni

The sequence BAB81138.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000016 Genomic DNA. Translation: BAB81138.1. Different initiation.
RefSeqiNP_562348.1. NC_003366.1.

Genome annotation databases

EnsemblBacteriaiBAB81138; BAB81138; BAB81138.
GeneIDi989742.
KEGGicpe:CPE1432.
PATRICi19496813. VBICloPer59675_1502.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000016 Genomic DNA. Translation: BAB81138.1 . Different initiation.
RefSeqi NP_562348.1. NC_003366.1.

3D structure databases

ProteinModelPortali P0C2D9.
SMRi P0C2D9. Positions 3-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 195102.CPE1432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB81138 ; BAB81138 ; BAB81138 .
GeneIDi 989742.
KEGGi cpe:CPE1432.
PATRICi 19496813. VBICloPer59675_1502.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci CPER195102:GJFM-1478-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 13 / Type A.

Entry informationi

Entry nameiGSA_CLOPE
AccessioniPrimary (citable) accession number: P0C2D9
Secondary accession number(s): Q9ZNC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 57 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