NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 4718 / IFO 12664 / LMG 139 / CIP 104326;
DOI=10.1007/BF00273610; PubMed=2034217 [NCBI, ExPASy, EBI, Israel, Japan]
Drolet M., Sasarman A.;
"Cloning and nucleotide sequence of the hemA gene of Agrobacterium radiobacter.";
Mol. Gen. Genet. 226:250-256(1991).

Comments

CATALYTIC ACTIVITY: Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO₂.
COFACTOR: Pyridoxal phosphate.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1 .
SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

S15996; S15996.

3D structure databases

HSSP

P07912; 1FC4. [HSSP ENTRY / PDB]

ModBase

P26505.

Ontologies

GO:0003870;	Molecular function: 5-aminolevulinate synthase activity (inferred from electronic annotation from InterPro).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0016769;	Molecular function: transferase activity, transferring nitrogenous groups (inferred from electronic annotation from InterPro).
GO:0006783;	Biological process: heme biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR010961; 4pyrrol_synth_NH2levulA_synth.
IPR004839; Aminotrans_I/II.
IPR001917; Aminotrans_II_pyridoxalP_BS.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.

Pfam

PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01821; 5aminolev_synth; 1.

PROSITE

PS00599; AA_TRANSFER_CLASS_2; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Heme biosynthesis; Pyridoxal phosphate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 405`	`405`	`5-aminolevulinate synthase.`	`PRO_0000163824`
`BINDING`	`248 248`		`Pyridoxal phosphate (covalent) (Probable).`

Sequence information

Length: 405 AA [This is the length of the unprocessed precursor]

Molecular weight: 44412 Da [This is the MW of the unprocessed precursor]

CRC64: F173AC1B13CAACDA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDFEAFFTTE LQSLHSEGRY RVFADIERQQ GNFPRATRYN ANGQRKDVTV WCSNDYLGMG 

        70         80         90        100        110        120 
QNPKVIEAMK AAIDHCGAGA GGTRNISGTN HYHVLLEQEL ADLHGKESAL IFTSGYVSNW 

       130        140        150        160        170        180 
ATLGTLGQKI PGLIIFSDAL NHASMIEGIR YGRCERVIWK HNDLEDLEAK LKAADPNAPK 

       190        200        210        220        230        240 
LIAFESVYSM DGDIAPIKEI CDLADRYGAM TYLDEVHAVG MYGPRGGGIA EREGLMDRLT 

       250        260        270        280        290        300 
IIEGTLGKAF GVMGGYITGS TAVCDFIRSF ASGFIFTTAL PPSLAAGAIA SIQHLKASPF 

       310        320        330        340        350        360 
ERARHQDRVR KLRGLLDARG IPHMDNPSHI VPVMVGDAAK CKWISDILLD SHGVYVQPIN 

       370        380        390        400 
YPTVPRKTER LRITPTPLHS DADIEHLVGA LHQLWSHCAL ARAVA

P26505 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools