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P24630

- GSA_SYNP6

UniProt

P24630 - GSA_SYNP6

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Protein
Glutamate-1-semialdehyde 2,1-aminomutase
Gene
hemL, gsa, syc0881_c
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.

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 Reviewed prediction 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
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 433432Glutamate-1-semialdehyde 2,1-aminomutaseUniRule annotation
PRO_0000120461Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi269084.syc0881_c.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GSAX-ray2.40A/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.

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

MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA    50
YAWDVDGNRY IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE 100
NVLAEMVIDA VPSIEMVRFV NSGTEACMAV LRLMRAYTGR DKIIKFEGCY 150
HGHADMFLVK AGSGVATLGL PDSPGVPKST TANTLTAPYN DLEAVKALFA 200
ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA LLVFDEVMTG 250
FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM 300
YQAGTLSGNP LAMTAGIKTL ELLRQPATYE YLDQITKRLS DGLLAIAQET 350
GHAACGGQVS GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL 400
APSQFEAGFT SLAHTEEDID ATLAAARTVM SAL 433
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511Y → I1 Publication
Sequence conflicti51 – 511Y → I1 Publication
Sequence conflicti108 – 1081I → N1 Publication
Sequence conflicti108 – 1081I → N1 Publication
Sequence conflicti133 – 1342LM → VV1 Publication
Sequence conflicti133 – 1342LM → VV1 Publication
Sequence conflicti172 – 1721D → S1 Publication
Sequence conflicti172 – 1721D → S1 Publication
Sequence conflicti179 – 1791S → K1 Publication
Sequence conflicti179 – 1791S → K1 Publication
Sequence conflicti187 – 1871A → T1 Publication
Sequence conflicti187 – 1871A → T1 Publication
Sequence conflicti327 – 3271A → G1 Publication
Sequence conflicti327 – 3271A → G1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X53695 Genomic DNA. Translation: CAA37733.1 .
AP008231 Genomic DNA. Translation: BAD79071.1 . Different initiation.
PIRi S13326.
RefSeqi YP_171591.2. NC_006576.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GSA X-ray 2.40 A/B 2-433 [» ]
3FQ7 X-ray 2.15 A/B 7-433 [» ]
3FQ8 X-ray 2.00 A/B 7-433 [» ]
3FQA X-ray 2.35 A/B 7-433 [» ]
3GSB X-ray 3.00 A/B 2-433 [» ]
4GSA X-ray 2.50 A/B 2-433 [» ]
ProteinModelPortali P24630.
SMRi P24630. Positions 7-433.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 269084.syc0881_c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD79071 ; BAD79071 ; syc0881_c .
GeneIDi 3199069.
KEGGi syc:syc0881_c.
PATRICi 32487518. VBISynElo117686_1027.

Phylogenomic databases

eggNOGi COG0001.
HOGENOMi HOG000020210.
KOi K01845.
OrthoDBi EOG6QVRHN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00317 .
UPA00668 .
BioCyci SELO269084:GCDQ-897-MONOMER.

Miscellaneous databases

EvolutionaryTracei P24630.

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. "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: June 11, 2014
This is version 114 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

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