Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

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

BioCyciSELO269084:GCDQ-897-MONOMER.
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 lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001175: Chromosome

Subcellular locationi

Cytoplasm Curated

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
Initiator methioninei1 – 11Removed
Chaini2 – 433432Glutamate-1-semialdehyde 2,1-aminomutasePRO_0000120461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi269084.syc0881_c.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Turni20 – 223Combined sources
Helixi24 – 263Combined sources
Beta strandi27 – 293Combined sources
Helixi30 – 334Combined sources
Turni35 – 384Combined sources
Beta strandi44 – 496Combined sources
Beta strandi51 – 544Combined sources
Beta strandi59 – 646Combined sources
Helixi65 – 673Combined sources
Turni68 – 725Combined sources
Helixi77 – 8711Combined sources
Helixi98 – 11013Combined sources
Beta strandi115 – 1228Combined sources
Helixi123 – 13816Combined sources
Beta strandi142 – 1476Combined sources
Helixi155 – 1573Combined sources
Helixi164 – 1685Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi174 – 1763Combined sources
Helixi178 – 1814Combined sources
Beta strandi184 – 1885Combined sources
Helixi192 – 20110Combined sources
Turni203 – 2053Combined sources
Beta strandi206 – 2116Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi217 – 2193Combined sources
Helixi227 – 23711Combined sources
Beta strandi241 – 2455Combined sources
Turni247 – 2526Combined sources
Helixi257 – 2615Combined sources
Beta strandi267 – 2715Combined sources
Helixi273 – 2764Combined sources
Beta strandi277 – 2804Combined sources
Beta strandi282 – 2865Combined sources
Helixi288 – 2914Combined sources
Turni295 – 2973Combined sources
Beta strandi298 – 3003Combined sources
Turni305 – 3084Combined sources
Helixi310 – 32314Combined sources
Helixi328 – 34922Combined sources
Beta strandi355 – 3595Combined sources
Beta strandi362 – 3698Combined sources
Helixi375 – 3784Combined sources
Helixi383 – 39513Combined sources
Helixi416 – 43217Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24630.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
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.

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 BAD79071.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511Y → I (PubMed:1900346).Curated
Sequence conflicti51 – 511Y → I (PubMed:1905724).Curated
Sequence conflicti108 – 1081I → N (PubMed:1900346).Curated
Sequence conflicti108 – 1081I → N (PubMed:1905724).Curated
Sequence conflicti133 – 1342LM → VV (PubMed:1900346).Curated
Sequence conflicti133 – 1342LM → VV (PubMed:1905724).Curated
Sequence conflicti172 – 1721D → S (PubMed:1900346).Curated
Sequence conflicti172 – 1721D → S (PubMed:1905724).Curated
Sequence conflicti179 – 1791S → K (PubMed:1900346).Curated
Sequence conflicti179 – 1791S → K (PubMed:1905724).Curated
Sequence conflicti187 – 1871A → T (PubMed:1900346).Curated
Sequence conflicti187 – 1871A → T (PubMed:1905724).Curated
Sequence conflicti327 – 3271A → G (PubMed:1900346).Curated
Sequence conflicti327 – 3271A → G (PubMed:1905724).Curated

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.
RefSeqiYP_171591.2. NC_006576.1.

Genome annotation databases

EnsemblBacteriaiBAD79071; BAD79071; syc0881_c.
GeneIDi3199069.
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.
RefSeqiYP_171591.2. NC_006576.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 7-433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi269084.syc0881_c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD79071; BAD79071; syc0881_c.
GeneIDi3199069.
KEGGisyc:syc0881_c.
PATRICi32487518. VBISynElo117686_1027.

Phylogenomic databases

eggNOGiCOG0001.
HOGENOMiHOG000020210.
KOiK01845.
OrthoDBiEOG6QVRHN.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00317.
UPA00668.
BioCyciSELO269084:GCDQ-897-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP24630.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli."
    Grimm B., Bull A., Breu V.
    Mol. Gen. Genet. 225:1-10(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of Synechococcus. Deletion of a tripeptide close to the NH2 terminus and internal amino acid substitution."
    Grimm B., Smith A.J., Kannangara C.G., Smith M.
    J. Biol. Chem. 266:12495-12501(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
    Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
    Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
  4. "Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus."
    Grimm B., Bull A., Welinder K.G., Gough S.P., Kannangara C.G.
    Carlsberg Res. Commun. 54:67-79(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-17.
  5. "Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity."
    Hennig M., Grimm B., Contestabile R., John R.A., Jansonius J.N.
    Proc. Natl. Acad. Sci. U.S.A. 94:4866-4871(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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: January 7, 2015
This is version 118 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

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.