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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMMAR368407:GH7L-1000-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:Memar_0982
OrganismiMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
Taxonomic identifieri368407 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus
ProteomesiUP000002146 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000382405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi368407.Memar_0982.

Structurei

3D structure databases

ProteinModelPortaliA3CU65.
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.

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.

A3CU65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSSELFNRA KTLMPGGVSS PVRAIKPYPF YVERAAGSHL TTVDGADLID
60 70 80 90 100
CCLGYGPLIL GHAHPEVREA IERQLEKGWL YGTPTPLELD LAGIITGDHP
110 120 130 140 150
AVEMVRFVSS GSEATMAAIR LARGYTGKQD IIKIEGGFHG AHDAVLVKAG
160 170 180 190 200
SGATTLGVPD SAGVLADLTA HTRQVPYNDT EALEALLAGN DDVAAFILEP
210 220 230 240 250
VMGNVGPVLP DDGYLADVRE ITAAHDVLLI LDEVITGYRA GIGGAEVLYD
260 270 280 290 300
VKPDLATFGK IIGGGLPIGA FGGRCDIMEL VAPAGPVYQA GTFSGNPASL
310 320 330 340 350
AAGYATLRHL HDHPEIYRRL DDATRAIGEA AADAGKGTFV RIGSLFKHFF
360 370 380 390 400
RDAAPRDYRE VKECDTEAFS RFWKAMLEAG IFLPPSQFET NFLSAAHTTQ
410
DIKQIAEAYG SCLFA
Length:415
Mass (Da):44,141
Last modified:March 20, 2007 - v1
Checksum:iBDBC7DA362E30F37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000562 Genomic DNA. Translation: ABN56915.1.
RefSeqiWP_011843826.1. NC_009051.1.
YP_001046897.1. NC_009051.1.

Genome annotation databases

EnsemblBacteriaiABN56915; ABN56915; Memar_0982.
GeneIDi4846259.
KEGGimem:Memar_0982.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000562 Genomic DNA. Translation: ABN56915.1.
RefSeqiWP_011843826.1. NC_009051.1.
YP_001046897.1. NC_009051.1.

3D structure databases

ProteinModelPortaliA3CU65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi368407.Memar_0982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN56915; ABN56915; Memar_0982.
GeneIDi4846259.
KEGGimem:Memar_0982.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OMAiCGHAHPE.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
BioCyciMMAR368407:GH7L-1000-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: ATCC 35101 / DSM 1498 / JR1.

Entry informationi

Entry nameiGSA_METMJ
AccessioniPrimary (citable) accession number: A3CU65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: March 20, 2007
Last modified: May 27, 2015
This is version 64 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

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.