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Protein

5-aminolevulinate synthase 2

Gene

hemT

Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
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

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from glycine.
Proteins known to be involved in this subpathway in this organism are:
  1. 5-aminolevulinate synthase 1 (hemA), 5-aminolevulinate synthase 2 (hemT)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from glycine, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei21 – 211SubstrateBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Binding sitei189 – 1891Pyridoxal phosphateBy similarity
Binding sitei217 – 2171Pyridoxal phosphateBy similarity
Binding sitei245 – 2451Pyridoxal phosphateBy similarity
Active sitei248 – 2481By similarity
Binding sitei277 – 2771Pyridoxal phosphateBy similarity
Binding sitei278 – 2781Pyridoxal phosphateBy similarity
Binding sitei363 – 3631SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13234.
RSPH272943:GJAS-3162-MONOMER.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase 2 (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemT
Ordered Locus Names:RHOS4_30750
ORF Names:RSP_3028
OrganismiRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Taxonomic identifieri272943 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000002703 Componenti: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4074075-aminolevulinate synthase 2PRO_0000163830Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481N6-(pyridoxal phosphate)lysineBy similarity

Interactioni

Protein-protein interaction databases

STRINGi272943.RSP_3028.

Structurei

3D structure databases

ProteinModelPortaliQ06965.
SMRiQ06965. Positions 2-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
KOiK00643.
OMAiRHGALTY.
OrthoDBiEOG6Q8HZD.
PhylomeDBiQ06965.

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.

Q06965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFSQHFQKL IDDMRLDGRY RTFAELERIA GEFPTALWHG PDGQARRVTV
60 70 80 90 100
WCSNDYLGMG QNAEVLAAMH RSIDLSGAGT GGTRNISGTN RQHVALEAEL
110 120 130 140 150
ADLHGKESAL IFTSGWISNL AALGTLGKIL PECAIFSDAL NHNSMIEGIR
160 170 180 190 200
RSGAERFIFH HNDPVHLDRL LSSVDPARPK IVAFESVYSM DGDIAPIAEI
210 220 230 240 250
CDVAERHGAL TYLDEVHAVG LYGPRGGGIS DRDGLADRVT IIEGTLAKAF
260 270 280 290 300
GVMGGYVSGP SLLMDVIRSM SDSFIFTTSI CPHLAAGALA AVRHVKAHPD
310 320 330 340 350
ERRRQAENAV RLKVLLQKAG LPVLDTPSHI LPVMVGEAHL CRSISEALLA
360 370 380 390 400
RHAIYVQPIN YPTVARGQER FRLTPTPFHT TSHMEALVEA LLAVGRDLGW

AMSRRAA
Length:407
Mass (Da):44,333
Last modified:October 1, 1996 - v1
Checksum:i4772E3EC1DA55D82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07489 Genomic DNA. Translation: AAA26124.1.
CP000144 Genomic DNA. Translation: ABA80643.1.
PIRiA49845.
RefSeqiWP_011338981.1. NZ_AKVW01000002.1.
YP_354544.1. NC_007494.2.

Genome annotation databases

EnsemblBacteriaiABA80643; ABA80643; RSP_3028.
GeneIDi3721613.
KEGGirsp:RSP_3028.
PATRICi23156193. VBIRhoSph57909_3445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07489 Genomic DNA. Translation: AAA26124.1.
CP000144 Genomic DNA. Translation: ABA80643.1.
PIRiA49845.
RefSeqiWP_011338981.1. NZ_AKVW01000002.1.
YP_354544.1. NC_007494.2.

3D structure databases

ProteinModelPortaliQ06965.
SMRiQ06965. Positions 2-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272943.RSP_3028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA80643; ABA80643; RSP_3028.
GeneIDi3721613.
KEGGirsp:RSP_3028.
PATRICi23156193. VBIRhoSph57909_3445.

Phylogenomic databases

eggNOGiCOG0156.
HOGENOMiHOG000221020.
KOiK00643.
OMAiRHGALTY.
OrthoDBiEOG6Q8HZD.
PhylomeDBiQ06965.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00375.
BioCyciMetaCyc:MONOMER-13234.
RSPH272943:GJAS-3162-MONOMER.

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. "Expression of the Rhodobacter sphaeroides hemA and hemT genes, encoding two 5-aminolevulinic acid synthase isozymes."
    Neidle E.L., Kaplan S.
    J. Bacteriol. 175:2292-2303(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."
    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.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Entry informationi

Entry nameiHEM0_RHOS4
AccessioniPrimary (citable) accession number: Q06965
Secondary accession number(s): Q3IXU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 7, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

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.