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P48247

- GSA_PSEAE

UniProt

P48247 - GSA_PSEAE

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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-4-amino-5-oxopentanoate = 5-aminolevulinate.

Cofactori

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

UniPathwayiUPA00251; UER00317.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase (EC:5.4.3.8)
Short name:
GSA
Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name:
GSA-AT
Gene namesi
Name:hemL
Ordered Locus Names:PA3977
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA3977.

Subcellular locationi

Cytoplasm Curated

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 – 427427Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120433Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi208964.PA3977.

Structurei

3D structure databases

ProteinModelPortaliP48247.
SMRiP48247. Positions 1-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
InParanoidiP48247.
KOiK01845.
OMAiRAIKPYP.
OrthoDBiEOG6QVRHN.
PhylomeDBiP48247.

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.

P48247-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRSETLFNN AQKHIPGGVN SPVRAFKSVG GTPLFFKHAE GAYVLDEDDK
60 70 80 90 100
RYVDYVGSWG PMILGHSHPD VLDAVRRQLD HGLSYGAPTA LEVEMADLVC
110 120 130 140 150
SMVPSMEMVR MVSSGTEATM SAIRLARGYT GRDSIIKFEG CYHGHSDSLL
160 170 180 190 200
VKAGSGALTF GVPNSPGVPA AFAKHTLTLP FNDIEAVRKT LGEVGKEVAC
210 220 230 240 250
IIVEPVAGNM NCVPPAPGFL EGLREACDEH GVVLIFDEVM TGFRVALGGA
260 270 280 290 300
QAYYGVTPDL STFGKIIGGG MPVGAFGGKR EIMQQISPLG PVYQAGTLSG
310 320 330 340 350
NPLAMAAGLT TLRLISRPGF HDELTAYTTR MLDGLQQRAD AAGIPFVTTQ
360 370 380 390 400
AGGMFGLYFS GADAIVTFED VMASDVERFK RFFHLMLDGG VYLAPSAFEA
410 420
GFTSIAHGDK ELEITLNAAE KAFAALK
Length:427
Mass (Da):45,398
Last modified:December 8, 2000 - v2
Checksum:i670EB87D144E2D28
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571A → S in CAA57575. (PubMed:7565600)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82072 Genomic DNA. Translation: CAA57575.1.
AE004091 Genomic DNA. Translation: AAG07364.1.
PIRiG83149.
S57898.
RefSeqiNP_252666.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG07364; AAG07364; PA3977.
GeneIDi880859.
KEGGipae:PA3977.
PATRICi19842625. VBIPseAer58763_4169.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82072 Genomic DNA. Translation: CAA57575.1 .
AE004091 Genomic DNA. Translation: AAG07364.1 .
PIRi G83149.
S57898.
RefSeqi NP_252666.1. NC_002516.2.

3D structure databases

ProteinModelPortali P48247.
SMRi P48247. Positions 1-426.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA3977.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG07364 ; AAG07364 ; PA3977 .
GeneIDi 880859.
KEGGi pae:PA3977.
PATRICi 19842625. VBIPseAer58763_4169.

Organism-specific databases

PseudoCAPi PA3977.

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
InParanoidi P48247.
KOi K01845.
OMAi RAIKPYP.
OrthoDBi EOG6QVRHN.
PhylomeDBi P48247.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .

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. "Cloning, mapping and characterization of the Pseudomonas aeruginosa hemL gene."
    Hungerer C., Troup B., Romling U., Jahn D.
    Mol. Gen. Genet. 248:375-380(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiGSA_PSEAE
AccessioniPrimary (citable) accession number: P48247
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 8, 2000
Last modified: November 26, 2014
This is version 112 of the entry and version 2 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