[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=8468290 [NCBI, ExPASy, EBI, Israel, Japan] Neidle E.L., Kaplan S.; "Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes."; J. Bacteriol. 175:2292-2303(1993).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.; "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.

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.
CAUTION: Expressed in the mutant strain HemA1 but expression in the wild-type strain has not been proven.

Copyright

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

Cross-references

Sequence databases

EMBL

L07489; AAA26124.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000144; ABA80643.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49845; A49845.

RefSeq

YP_354544.1; -.

3D structure databases

HSSP

P07912; 1FC4. [HSSP ENTRY / PDB]

ModBase

Q06965.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13234; -.
RSPH272943:RSP_3028-MON; -.

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.

Genome annotation databases

GeneID

3721613; -.

GenomeReviews

CP000144_GR; RHOS4_30750.

KEGG

rsp:RSP_3028; -.

NMPDR

fig|272943.3.peg.3643; -.

Phylogenomic databases

HOGENOM

Q06965; -.

Genome annotation databases

CMR

Q06965; RHOS4_30750.

Other

UniRef

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

Keywords

Acyltransferase; Complete proteome; Heme biosynthesis; Pyridoxal phosphate; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 407`	`407`	`5-aminolevulinate synthase 2.`	`PRO_0000163830`
`BINDING`	`248 248`		`Pyridoxal phosphate (covalent) (By similarity).`

Sequence information

Length: 407 AA [This is the length of the unprocessed precursor]

Molecular weight: 44333 Da [This is the MW of the unprocessed precursor]

CRC64: 4772E3EC1DA55D82 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEFSQHFQKL IDDMRLDGRY RTFAELERIA GEFPTALWHG PDGQARRVTV WCSNDYLGMG 

        70         80         90        100        110        120 
QNAEVLAAMH RSIDLSGAGT GGTRNISGTN RQHVALEAEL ADLHGKESAL IFTSGWISNL 

       130        140        150        160        170        180 
AALGTLGKIL PECAIFSDAL NHNSMIEGIR RSGAERFIFH HNDPVHLDRL LSSVDPARPK 

       190        200        210        220        230        240 
IVAFESVYSM DGDIAPIAEI CDVAERHGAL TYLDEVHAVG LYGPRGGGIS DRDGLADRVT 

       250        260        270        280        290        300 
IIEGTLAKAF GVMGGYVSGP SLLMDVIRSM SDSFIFTTSI CPHLAAGALA AVRHVKAHPD 

       310        320        330        340        350        360 
ERRRQAENAV RLKVLLQKAG LPVLDTPSHI LPVMVGEAHL CRSISEALLA RHAIYVQPIN 

       370        380        390        400 
YPTVARGQER FRLTPTPFHT TSHMEALVEA LLAVGRDLGW AMSRRAA

Q06965 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