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Protein

5-aminolevulinate synthase

Gene

hemA

Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 Publication

Pathwayi: 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 (hemA)
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)DescriptionActionsGraphical viewLength
Binding sitei21Substrate1 Publication1
Binding sitei137Substrate1 Publication1
Binding sitei156Substrate1 Publication1
Binding sitei189Pyridoxal phosphate1 Publication1
Binding sitei217Pyridoxal phosphate1 Publication1
Binding sitei245Pyridoxal phosphate1 Publication1
Active sitei2481 Publication1
Binding sitei277Pyridoxal phosphate; shared with dimeric partner1 Publication1
Binding sitei278Pyridoxal phosphate; shared with dimeric partner1 Publication1
Binding sitei365Substrate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processHeme biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.3.1.37 5381
UniPathwayiUPA00251; UER00375

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase (EC:2.3.1.37)
Alternative name(s):
5-aminolevulinic acid synthase
Delta-ALA synthase
Delta-aminolevulinate synthase
Gene namesi
Name:hemA
Ordered Locus Names:RCAP_rcc01447
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002361 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001638281 – 4095-aminolevulinate synthaseAdd BLAST409

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei248N6-(pyridoxal phosphate)lysineCurated1

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi272942.RCAP_rcc01447

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 16Combined sources14
Beta strandi25 – 28Combined sources4
Beta strandi35 – 39Combined sources5
Beta strandi45 – 50Combined sources6
Helixi59 – 61Combined sources3
Helixi63 – 76Combined sources14
Turni84 – 86Combined sources3
Helixi91 – 103Combined sources13
Beta strandi107 – 113Combined sources7
Helixi115 – 129Combined sources15
Beta strandi134 – 138Combined sources5
Helixi143 – 151Combined sources9
Beta strandi156 – 159Combined sources4
Helixi164 – 173Combined sources10
Beta strandi180 – 187Combined sources8
Turni189 – 191Combined sources3
Helixi197 – 207Combined sources11
Beta strandi210 – 214Combined sources5
Turni216 – 221Combined sources6
Helixi229 – 233Combined sources5
Helixi236 – 238Combined sources3
Beta strandi240 – 248Combined sources9
Beta strandi255 – 259Combined sources5
Helixi261 – 270Combined sources10
Helixi272 – 275Combined sources4
Helixi282 – 295Combined sources14
Helixi298 – 321Combined sources24
Beta strandi329 – 331Combined sources3
Beta strandi333 – 336Combined sources4
Helixi340 – 354Combined sources15
Turni363 – 365Combined sources3
Beta strandi372 – 375Combined sources4
Helixi383 – 396Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BWNX-ray2.10A/B/D/E1-401[»]
2BWOX-ray2.80A/B/D/E1-401[»]
2BWPX-ray2.70A/B/D/E1-401[»]
ProteinModelPortaliP18079
SMRiP18079
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18079

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107EEK Bacteria
COG0156 LUCA
HOGENOMiHOG000221020
KOiK00643
OMAiATPINYP
OrthoDBiPOG091H024U

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
InterProiView protein in InterPro
IPR010961 4pyrrol_synth_NH2levulA_synth
IPR001917 Aminotrans_II_pyridoxalP_BS
IPR004839 Aminotransferase_I/II
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01821 5aminolev_synth, 1 hit
PROSITEiView protein in PROSITE
PS00599 AA_TRANSFER_CLASS_2, 1 hit

Sequencei

Sequence statusi: Complete.

P18079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYNLALDKA IQKLHDEGRY RTFIDIEREK GAFPKAQWNR PDGGKQDITV
60 70 80 90 100
WCGNDYLGMG QHPVVLAAMH EALEAVGAGS GGTRNISGTT AYHRRLEAEI
110 120 130 140 150
ADLHGKEAAL VFSSAYIAND ATLSTLRVLF PGLIIYSDSL NHASMIEGIK
160 170 180 190 200
RNAGPKRIFR HNDVAHLREL IAADDPAAPK LIAFESVYSM DGDFGPIKEI
210 220 230 240 250
CDIADEFGAL TYIDEVHAVG MYGPRGAGVA ERDGLMHRID IFNGTLAKAY
260 270 280 290 300
GVFGGYIAAS AKMVDAVRSY APGFIFSTSL PPAIAAGAQA SIAFLKTAEG
310 320 330 340 350
QKLRDAQQMH AKVLKMRLKA LGMPIIDHGS HIVPVVIGDP VHTKAVSDML
360 370 380 390 400
LSDYGVYVQP INFPTVPRGT ERLRFTPSPV HDLKQIDGLV HAMDLLWARC

ALNRAEASA
Length:409
Mass (Da):44,374
Last modified:May 31, 2011 - v2
Checksum:iFCC89DA6EBA8DFB3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128V → L in CAA37857 (PubMed:2381418).Curated1
Sequence conflicti128V → L in CAA37393 (PubMed:1904045).Curated1
Sequence conflicti402 – 409Missing in CAA37857 (PubMed:2381418).Curated8
Sequence conflicti402 – 409Missing in CAA37393 (PubMed:1904045).Curated8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53309 Genomic DNA Translation: CAA37393.1
X53864 Genomic DNA Translation: CAA37857.1
CP001312 Genomic DNA Translation: ADE85192.1
PIRiS10528
RefSeqiWP_013067171.1, NC_014034.1

Genome annotation databases

EnsemblBacteriaiADE85192; ADE85192; RCAP_rcc01447
GeneIDi31490330
KEGGircp:RCAP_rcc01447

Similar proteinsi

Entry informationi

Entry nameiHEM1_RHOCB
AccessioniPrimary (citable) accession number: P18079
Secondary accession number(s): D5AT85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 31, 2011
Last modified: March 28, 2018
This is version 119 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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