P24630 (GSA_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate-1-semialdehyde 2,1-aminomutase
Short name=GSA
EC=5.4.3.8

Alternative name(s):
Glutamate-1-semialdehyde aminotransferase
Short name=GSA-AT

Gene names

Name:	hemL
Synonyms:	gsa
Ordered Locus Names:	syc0881_c

Organism

Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]

Taxonomic identifier

269084 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus › Synechococcus elongatus

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375
Cofactor	Pyridoxal phosphate.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375 Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP-Rule MF_00375
Subunit structure	Homodimer.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_00375.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily.
Sequence caution	The sequence BAD79071.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutamate-1-semialdehyde 2,1-aminomutase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transaminase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 433

432

Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375

PRO_0000120461

Amino acid modifications

Modified residue

273

1

N6-(pyridoxal phosphate)lysine HAMAP-Rule MF_00375

Experimental info

Sequence conflict

51

1

Y → I Ref.1

Sequence conflict

51

1

Y → I Ref.2

Sequence conflict

108

1

I → N Ref.1

Sequence conflict

108

1

I → N Ref.2

Sequence conflict

133 – 134

2

LM → VV Ref.1

Sequence conflict

133 – 134

2

LM → VV Ref.2

Sequence conflict

172

1

D → S Ref.1

Sequence conflict

172

1

D → S Ref.2

Sequence conflict

179

1

S → K Ref.1

Sequence conflict

179

1

S → K Ref.2

Sequence conflict

187

1

A → T Ref.1

Sequence conflict

187

1

A → T Ref.2

Sequence conflict

327

1

A → G Ref.1

Sequence conflict

327

1

A → G Ref.2

Secondary structure

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433

Helix Strand Turn

Details...

Helix

10 – 19

10

Turn

20 – 22

3

Helix

24 – 26

3

Beta strand

27 – 29

3

Helix

30 – 33

4

Turn

35 – 38

4

Beta strand

44 – 49

6

Beta strand

51 – 54

4

Beta strand

59 – 64

6

Helix

65 – 67

3

Turn

68 – 72

5

Helix

77 – 87

11

Helix

98 – 110

13

Beta strand

115 – 122

8

Helix

123 – 138

16

Beta strand

142 – 147

6

Helix

155 – 157

3

Helix

164 – 168

5

Beta strand

174 – 176

3

Helix

178 – 181

4

Beta strand

184 – 188

5

Helix

192 – 201

10

Turn

203 – 205

3

Beta strand

206 – 211

6

Beta strand

213 – 215

3

Beta strand

217 – 219

3

Helix

227 – 237

11

Beta strand

241 – 245

5

Turn

247 – 252

6

Helix

257 – 261

5

Beta strand

267 – 271

5

Helix

273 – 276

4

Beta strand

277 – 280

4

Beta strand

282 – 286

5

Helix

288 – 291

4

Turn

295 – 297

3

Beta strand

298 – 300

3

Turn

305 – 308

4

Helix

310 – 323

14

Helix

328 – 349

22

Beta strand

355 – 359

5

Beta strand

362 – 369

8

Helix

375 – 378

4

Helix

383 – 395

13

Helix

416 – 432

17

Sequences

	Sequence		Length	Mass (Da)
	P24630 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 83585133A666B923	FASTA	433	46,116
	10 20 30 40 50 60 MVTSSPFKTI KSDEIFAAAQ KLMPGGVSSP VRAFKSVGGQ PIVFDRVKDA YAWDVDGNRY 70 80 90 100 110 120 IDYVGTWGPA ICGHAHPEVI EALKVAMEKG TSFGAPCALE NVLAEMVIDA VPSIEMVRFV 130 140 150 160 170 180 NSGTEACMAV LRLMRAYTGR DKIIKFEGCY HGHADMFLVK AGSGVATLGL PDSPGVPKST 190 200 210 220 230 240 TANTLTAPYN DLEAVKALFA ENPGEIAGVI LEPIVGNSGF IVPDAGFLEG LREITLEHDA 250 260 270 280 290 300 LLVFDEVMTG FRIAYGGVQE KFGVTPDLTT LGKIIGGGLP VGAYGGKREI MQLVAPAGPM 310 320 330 340 350 360 YQAGTLSGNP LAMTAGIKTL ELLRQPATYE YLDQITKRLS DGLLAIAQET GHAACGGQVS 370 380 390 400 410 420 GMFGFFFTEG PVHNYEDAKK SDLQKFSRFH RGMLEQGIYL APSQFEAGFT SLAHTEEDID 430 ATLAAARTVM SAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53695 Genomic DNA. Translation: CAA37733.1.
AP008231 Genomic DNA. Translation: BAD79071.1. Different initiation.

PIR

S13326.

RefSeq

YP_171591.2. NC_006576.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P24630.

SMR

P24630. Positions 7-433.

ModBase

Search...

Protein-protein interaction databases

STRING

269084.syc0881_c.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD79071; BAD79071; syc0881_c.

GeneID

3199069.

KEGG

syc:syc0881_c.

PATRIC

32487518. VBISynElo117686_1027.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0001.

HOGENOM

HOG000020210.

KO

K01845.

ProtClustDB

PRK00062.

Enzyme and pathway databases

UniPathway

UPA00251; UER00317.
UPA00668.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.

HAMAP

MF_00375. HemL_aminotrans_3.

InterPro

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]

PANTHER

PTHR11986. PTHR11986. 1 hit.
PTHR11986:SF5. PTHR11986:SF5. 1 hit.

Pfam

PF00202. Aminotran_3. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR00713. hemL. 1 hit.

PROSITE

PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P24630.

Entry information

Entry name

GSA_SYNP6

Accession

Primary (citable) accession number: P24630
Secondary accession number(s): Q5N3P9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 108 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program