Reviewed, UniProtKB/Swiss-Prot P43090 (HEM0_OPSTA)

Names and origin

Protein names

Recommended name:
    5-aminolevulinate synthase, erythroid-specific, mitochondrial
      Short name=ALAS-E
    EC=2.3.1.37
Alternative name(s):
    5-aminolevulinic acid synthase 2
    Delta-aminolevulinate synthase 2
    Delta-ALA synthase 2

Gene names

Name:

alas2

Organism

Opsanus tau (Oyster toadfish)

Taxonomic identifier

8068 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Paracanthopterygii › Batrachoididae › Opsanus

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (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.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix.
Miscellaneous	There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.
Sequence similarities	Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Biological process	Heme biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial inner membrane Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	5-aminolevulinate synthase activity Inferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 582		5-aminolevulinate synthase, erythroid-specific, mitochondrial		PRO_0000001228
Amino acid modifications
	Modified residue	386	1	N6-(pyridoxal phosphate)lysine Probable

Sequences

	Sequence		Length	Mass (Da)
	P43090-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: FB066EEF72E146C9	FASTA	582	64,531
	10 20 30 40 50 60 MAAFLHHCPF LKSMPKPALR RRVPALLSLA DRCPVIVHQV CISRLHILET KLDVSPTQPK 70 80 90 100 110 120 RQRLSLLDQK RLFAQTATQV AVSVSKGCPF VSSQIGMVRA SPEVQEDVQA DLKSPVLPTP 130 140 150 160 170 180 PQTGITQLLK DNMVGPSFDY DNFFNEKIAE KKRDHTYRVF KTVNRNAVVF PFAEDYSVSD 190 200 210 220 230 240 RQGSQVSVWC SNDYLGMSRH PRVLEAIREV LERHGAGAGG TRNISGTSKY HVTLEKELAH 250 260 270 280 290 300 LHQKDAALVF SSCFVANDST LFTLAKMLPG CHIYSDAGNH ASMIQGIRNS GAKRFIFRHN 310 320 330 340 350 360 DSRHLEELLQ QSDPKTPKIV AFETVHSMDG AICPLEELCD VAHRHGALTF VDEVHAVGLY 370 380 390 400 410 420 GAHGAGVGER DNVMHKIDIV SGTLGKAFGC VGGYVASSAA LVDTVRSFAA GFIFTTSLPP 430 440 450 460 470 480 MILAGALESV RVLKSPEGQL LRRAHQRNVK YMRQLLMDKG LPVVNCPSHI IPIRVGNAEL 490 500 510 520 530 540 NTKVCDSLLE KHNIYVQAIN YPTVPRGQEL LRLAPSPHHH PAMMEYFVDK LVEVWQEAGL 550 560 570 580 LLNGPATVSC TFCDRPLHFD LMSEWEKSYF GNMEPQYITM SA

References

[1]	"5-aminolevulinate synthase in the marine fish, Opsanus tau." Hellmich H.L., Cornell N.W. Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L02632 mRNA. Translation: AAA60729.1.
3D structure databases
SMR	P43090. Positions 139-535.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P43090.
Enzyme and pathway databases
BRENDA	2.3.1.37. 289317.
Family and domain databases
InterPro	IPR010961. 4pyrrol_synth_NH2levulA_synth. IPR001917. Aminotrans_II_pyridoxalP_BS. IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01821. 5aminolev_synth. 1 hit.
PROSITE	PS00599. AA_TRANSFER_CLASS_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM0_OPSTA

Accession

Primary (citable) accession number: P43090

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)