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Protein

Glutamate-1-semialdehyde 2,1-aminomutase

Gene

hemL

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
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 (GSA-AT), 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.

Pathwayi: chlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi5.4.3.8. 6187.
UniPathwayiUPA00251; UER00317.
UPA00668.

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
Synonyms:gsa
Ordered Locus Names:syc0881_c
OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Taxonomic identifieri269084 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001175 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001204612 – 433Glutamate-1-semialdehyde 2,1-aminomutaseAdd BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei273N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-61261N.
STRINGi269084.syc0881_c.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 19Combined sources10
Turni20 – 22Combined sources3
Helixi24 – 26Combined sources3
Beta strandi27 – 29Combined sources3
Helixi30 – 33Combined sources4
Turni35 – 38Combined sources4
Beta strandi44 – 49Combined sources6
Beta strandi51 – 54Combined sources4
Beta strandi59 – 64Combined sources6
Helixi65 – 67Combined sources3
Turni68 – 72Combined sources5
Helixi77 – 87Combined sources11
Helixi98 – 110Combined sources13
Beta strandi115 – 122Combined sources8
Helixi123 – 138Combined sources16
Beta strandi142 – 147Combined sources6
Helixi155 – 157Combined sources3
Helixi164 – 168Combined sources5
Beta strandi171 – 173Combined sources3
Beta strandi174 – 176Combined sources3
Helixi178 – 181Combined sources4
Beta strandi184 – 188Combined sources5
Helixi192 – 201Combined sources10
Turni203 – 205Combined sources3
Beta strandi206 – 211Combined sources6
Beta strandi213 – 215Combined sources3
Beta strandi217 – 219Combined sources3
Helixi227 – 237Combined sources11
Beta strandi241 – 245Combined sources5
Turni247 – 252Combined sources6
Helixi257 – 261Combined sources5
Beta strandi267 – 271Combined sources5
Helixi273 – 276Combined sources4
Beta strandi277 – 280Combined sources4
Beta strandi282 – 286Combined sources5
Helixi288 – 291Combined sources4
Turni295 – 297Combined sources3
Beta strandi298 – 300Combined sources3
Turni305 – 308Combined sources4
Helixi310 – 323Combined sources14
Helixi328 – 349Combined sources22
Beta strandi355 – 359Combined sources5
Beta strandi362 – 369Combined sources8
Helixi375 – 378Combined sources4
Helixi383 – 395Combined sources13
Helixi416 – 432Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GSAX-ray2.40A/B2-433[»]
2HOYX-ray2.20A/B2-433[»]
2HOZX-ray2.20A/B2-433[»]
2HP1X-ray2.08A/B2-433[»]
2HP2X-ray2.70A/B2-433[»]
3FQ7X-ray2.15A/B7-433[»]
3FQ8X-ray2.00A/B7-433[»]
3FQAX-ray2.35A/B7-433[»]
3GSBX-ray3.00A/B2-433[»]
4GSAX-ray2.50A/B2-433[»]
ProteinModelPortaliP24630.
SMRiP24630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24630.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.
OrthoDBiPOG091H04O1.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24630-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA
60 70 80 90 100
YAWDVDGNRY IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE
110 120 130 140 150
NVLAEMVIDA VPSIEMVRFV NSGTEACMAV LRLMRAYTGR DKIIKFEGCY
160 170 180 190 200
HGHADMFLVK AGSGVATLGL PDSPGVPKST TANTLTAPYN DLEAVKALFA
210 220 230 240 250
ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA LLVFDEVMTG
260 270 280 290 300
FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM
310 320 330 340 350
YQAGTLSGNP LAMTAGIKTL ELLRQPATYE YLDQITKRLS DGLLAIAQET
360 370 380 390 400
GHAACGGQVS GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL
410 420 430
APSQFEAGFT SLAHTEEDID ATLAAARTVM SAL
Length:433
Mass (Da):46,116
Last modified:January 23, 2007 - v4
Checksum:i83585133A666B923
GO

Sequence cautioni

The sequence BAD79071 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti51Y → I (PubMed:1900346).Curated1
Sequence conflicti51Y → I (PubMed:1905724).Curated1
Sequence conflicti108I → N (PubMed:1900346).Curated1
Sequence conflicti108I → N (PubMed:1905724).Curated1
Sequence conflicti133 – 134LM → VV (PubMed:1900346).Curated2
Sequence conflicti133 – 134LM → VV (PubMed:1905724).Curated2
Sequence conflicti172D → S (PubMed:1900346).Curated1
Sequence conflicti172D → S (PubMed:1905724).Curated1
Sequence conflicti179S → K (PubMed:1900346).Curated1
Sequence conflicti179S → K (PubMed:1905724).Curated1
Sequence conflicti187A → T (PubMed:1900346).Curated1
Sequence conflicti187A → T (PubMed:1905724).Curated1
Sequence conflicti327A → G (PubMed:1900346).Curated1
Sequence conflicti327A → G (PubMed:1905724).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53695 Genomic DNA. Translation: CAA37733.1.
AP008231 Genomic DNA. Translation: BAD79071.1. Different initiation.
PIRiS13326.
RefSeqiWP_011243193.1. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD79071; BAD79071; syc0881_c.
KEGGisyc:syc0881_c.
PATRICi32487518. VBISynElo117686_1027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53695 Genomic DNA. Translation: CAA37733.1.
AP008231 Genomic DNA. Translation: BAD79071.1. Different initiation.
PIRiS13326.
RefSeqiWP_011243193.1. NC_006576.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GSAX-ray2.40A/B2-433[»]
2HOYX-ray2.20A/B2-433[»]
2HOZX-ray2.20A/B2-433[»]
2HP1X-ray2.08A/B2-433[»]
2HP2X-ray2.70A/B2-433[»]
3FQ7X-ray2.15A/B7-433[»]
3FQ8X-ray2.00A/B7-433[»]
3FQAX-ray2.35A/B7-433[»]
3GSBX-ray3.00A/B2-433[»]
4GSAX-ray2.50A/B2-433[»]
ProteinModelPortaliP24630.
SMRiP24630.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61261N.
STRINGi269084.syc0881_c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD79071; BAD79071; syc0881_c.
KEGGisyc:syc0881_c.
PATRICi32487518. VBISynElo117686_1027.

Phylogenomic databases

eggNOGiENOG4105CDM. Bacteria.
COG0001. LUCA.
HOGENOMiHOG000020210.
KOiK01845.
OrthoDBiPOG091H04O1.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BRENDAi5.4.3.8. 6187.

Miscellaneous databases

EvolutionaryTraceiP24630.

Family and domain databases

CDDicd00610. OAT_like. 1 hit.
Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPiMF_00375. HemL_aminotrans_3. 1 hit.
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...

Entry informationi

Entry nameiGSA_SYNP6
AccessioniPrimary (citable) accession number: P24630
Secondary accession number(s): Q5N3P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.