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Protein

5-aminolevulinate synthase, mitochondrial

Gene

hemA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactori

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei170 – 1701SubstrateBy similarity
Binding sitei283 – 2831SubstrateBy similarity
Binding sitei302 – 3021SubstrateBy similarity
Binding sitei335 – 3351Pyridoxal phosphateBy similarity
Binding sitei363 – 3631Pyridoxal phosphateBy similarity
Binding sitei409 – 4091Pyridoxal phosphateBy similarity
Active sitei412 – 4121By similarity
Binding sitei441 – 4411Pyridoxal phosphateBy similarity
Binding sitei442 – 4421Pyridoxal phosphateBy similarity
Binding sitei527 – 5271SubstrateBy similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, mitochondrial (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemA
ORF Names:AN2284
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VII

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 6485-aminolevulinate synthase, mitochondrialPRO_0000001240
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei412 – 4121N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00008976.

Structurei

3D structure databases

ProteinModelPortaliP38092.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
InParanoidiP38092.
KOiK00643.
OMAiKLAQYPK.
OrthoDBiEOG7HHX1P.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38092-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEALLQQSRA MCPFLKRSSP NTLRSLATAT RPSTSPGGGT MTNLQRIARR
60 70 80 90 100
CPVMSKALAV QSARMTGTKR FTSSAAGVPG AGAGTPKPTR GSPGKRALHS
110 120 130 140 150
TGGNGANMST EFHKGAQQIH PGLSNATRSH VGASATVSGP TPRAPVAAPF
160 170 180 190 200
DYDAFYNAEL QKKHQDKSYR YFNNINRLAQ EFPRAHTASK DEKVTVWCSN
210 220 230 240 250
DYLGMGRNPE VLATMHKTLD TYGAGAGGTR NISGHNQHAV SLENTLAKLH
260 270 280 290 300
GKEAALVFSS CFVANDATLA TLGSKMPDCV ILSDSLNHAS MIQGIRHSGA
310 320 330 340 350
KKMVFKHNDL VDLETKLASL PLHVPKIIAF ESVYSMCGSI APIEAICDLA
360 370 380 390 400
DKYGAITFLD EVHAVGMYGP HGAGVAEHLD YEIYASQDTA NPLSTKGTVM
410 420 430 440 450
DRINIITGTL GKAYGCVGGY IAGSAALVDT IRSLAPGFIF TTSLPPATMA
460 470 480 490 500
GADTAIRYQA RHQQDRILQQ LHTRAVKQSF KDLDIPVIPN PSHIVPLLVG
510 520 530 540 550
DAELAKQASD KLLEEHGIYV QAINYPTVPR GEERLRITPT PGHTQELRDH
560 570 580 590 600
LVEAVNTVWN DLGIKRASDW KAMGGFVGVG VEAAELENQP IWTDAQLNMR
610 620 630 640
PDETLEAAVE REFQAAVPGM KAGGAKAKPV GSIAANPIGA SIPVAAAA
Length:648
Mass (Da):68,960
Last modified:May 26, 2009 - v2
Checksum:i1D450D773925F13F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001A → R in CAA45508 (PubMed:8319309).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64170 Genomic DNA. Translation: CAA45508.1.
AACD01000038 Genomic DNA. Translation: EAA64395.1.
BN001307 Genomic DNA. Translation: CBF86531.1.
PIRiS31846.
RefSeqiXP_659888.1. XM_654796.1.

Genome annotation databases

EnsemblFungiiCADANIAT00008976; CADANIAP00008976; CADANIAG00008976.
GeneIDi2874789.
KEGGiani:AN2284.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64170 Genomic DNA. Translation: CAA45508.1.
AACD01000038 Genomic DNA. Translation: EAA64395.1.
BN001307 Genomic DNA. Translation: CBF86531.1.
PIRiS31846.
RefSeqiXP_659888.1. XM_654796.1.

3D structure databases

ProteinModelPortaliP38092.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00008976.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00008976; CADANIAP00008976; CADANIAG00008976.
GeneIDi2874789.
KEGGiani:AN2284.2.

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
InParanoidiP38092.
KOiK00643.
OMAiKLAQYPK.
OrthoDBiEOG7HHX1P.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and nucleotide sequence of the 5-aminolevulinate synthase gene from Aspergillus nidulans."
    Bradshaw R.E., Dixon S.W.C., Raitt D.C., Pillar T.M.
    Curr. Genet. 23:501-507(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R153.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiHEM1_EMENI
AccessioniPrimary (citable) accession number: P38092
Secondary accession number(s): C8VN31, Q5BAZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 26, 2009
Last modified: April 1, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.