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Q0TQG7

- GSA_CLOP1

UniProt

Q0TQG7 - GSA_CLOP1

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Clostridium perfringens (strain ATCC 13124 / NCTC 8237 / 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

BioCyciCPER195103:GHAW-1702-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:CPF_1685
OrganismiClostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A)
Taxonomic identifieri195103 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001823: 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_0000273581Add
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

STRINGi195103.CPF_1685.

Structurei

3D structure databases

ProteinModelPortaliQ0TQG7.
SMRiQ0TQG7. 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.
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.

Q0TQG7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDRNKEIFEE SKKYMPGGVN SPVRSFGSVG INPPVIKSGK GAMIKDENGN
60 70 80 90 100
EYIDFVLAWG PMILGHCDED VVKAIKKTSE 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 YYDHIEKIGS KLEKGVLEIA KKKGLGLVVN
360 370 380 390 400
RQGGMMTLFF TDLKEVKCYD DVKTCDGERF KRYFLHMLNK GFNIPPSQFE
410 420
AMFLSVKHTE EHIDKFLEAF ESFEG
Length:425
Mass (Da):46,885
Last modified:September 5, 2006 - v1
Checksum:iF7DFA932D15F2267
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017186 Genomic DNA. Translation: BAA74784.1.
CP000246 Genomic DNA. Translation: ABG84031.1.
PIRiT43861.
RefSeqiWP_003481561.1. NC_008261.1.
YP_696123.1. NC_008261.1.

Genome annotation databases

EnsemblBacteriaiABG84031; ABG84031; CPF_1685.
GeneIDi4201829.
KEGGicpf:CPF_1685.
PATRICi19485620. VBICloPer106549_1629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017186 Genomic DNA. Translation: BAA74784.1 .
CP000246 Genomic DNA. Translation: ABG84031.1 .
PIRi T43861.
RefSeqi WP_003481561.1. NC_008261.1.
YP_696123.1. NC_008261.1.

3D structure databases

ProteinModelPortali Q0TQG7.
SMRi Q0TQG7. Positions 3-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 195103.CPF_1685.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG84031 ; ABG84031 ; CPF_1685 .
GeneIDi 4201829.
KEGGi cpf:CPF_1685.
PATRICi 19485620. VBICloPer106549_1629.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
BioCyci CPER195103:GHAW-1702-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

« Hide 'large scale' publications
  1. "A Clostridium perfringens hem gene cluster contains a cysG(B) homologue that is involved in cobalamin biosynthesis."
    Koyama M., Katayama S., Kaji M., Taniguchi Y., Matsushita O., Minami J., Morita S., Okabe A.
    Microbiol. Immunol. 43:947-957(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13124 / NCTC 8237 / Type A.

Entry informationi

Entry nameiGSA_CLOP1
AccessioniPrimary (citable) accession number: Q0TQG7
Secondary accession number(s): Q9ZNC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: September 5, 2006
Last modified: November 26, 2014
This is version 65 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