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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Prochlorococcus marinus (strain MIT 9211)
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

BioCyciPMAR93059:GHJV-503-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:P9211_04841
OrganismiProchlorococcus marinus (strain MIT 9211)
Taxonomic identifieri93059 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000000788 Componenti: 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_1000121908Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei271 – 2711N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiA9BEA5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi93059.P9211_04841.

Structurei

3D structure databases

ProteinModelPortaliA9BEA5.
SMRiA9BEA5. Positions 5-431.
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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A9BEA5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNAFNTNLS QAVFNAAQDL MPGGVSSPVR AFKSVNGDPI VFDRVKGPYA
60 70 80 90 100
WDLDGNRFID YVGSWGPAIC GHSHPEVIAA LQEALEKGTS FGAPCELENK
110 120 130 140 150
LAGMVIEAVP SVEMVRFVNS GTEACMAVLR LMRAFTGRDK LIKFEGCYHG
160 170 180 190 200
HADMFLVKAG SGVATLGLPD SPGVPRSTTS NTLTAPYNDL EAVKALFAEN
210 220 230 240 250
PDAISGVILE PIVGNAGFIP PEPGFLEGLR ELTKENGSLL VFDEVMTGFR
260 270 280 290 300
ISYGGAQERF GVTPDLTTMG KVIGGGLPVG AYGGRKEIMS MVAPAGPMYQ
310 320 330 340 350
AGTLSGNPLA MTAGIKTLEL LKQEGTYERL ESLSQRLING ICESAKKAGI
360 370 380 390 400
PITGSFISGM FGFYLCEGPV RNFQEAKQTN AELFGKLHRA MLEKGIYLAP
410 420 430
SAFEAGFTSL AHSNDDIETT IKAFEASFSE IV
Length:432
Mass (Da):45,991
Last modified:January 15, 2008 - v1
Checksum:i68892D14BE0F3232
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000878 Genomic DNA. Translation: ABX08415.1.
RefSeqiWP_012195038.1. NC_009976.1.
YP_001550369.1. NC_009976.1.

Genome annotation databases

EnsemblBacteriaiABX08415; ABX08415; P9211_04841.
KEGGipmj:P9211_04841.
PATRICi22986462. VBIProMar136502_0514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000878 Genomic DNA. Translation: ABX08415.1.
RefSeqiWP_012195038.1. NC_009976.1.
YP_001550369.1. NC_009976.1.

3D structure databases

ProteinModelPortaliA9BEA5.
SMRiA9BEA5. Positions 5-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93059.P9211_04841.

Proteomic databases

PRIDEiA9BEA5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX08415; ABX08415; P9211_04841.
KEGGipmj:P9211_04841.
PATRICi22986462. VBIProMar136502_0514.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciPMAR93059:GHJV-503-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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00713. hemL. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9211.

Entry informationi

Entry nameiGSA_PROM4
AccessioniPrimary (citable) accession number: A9BEA5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: April 1, 2015
This is version 61 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

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.