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Protein

Aldehyde decarbonylase

Gene

PMT_1231

Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the decarbonylation of fatty aldehydes to alkanes. Requires the presence of ferredoxin, ferredoxin reductase and NADPH for in vitro decarbonylase activity (By similarity). Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane.UniRule annotation1 Publication

Catalytic activityi

A long-chain aldehyde + O2 + 2 NADPH = an alkane + formate + H2O + 2 NADP+.UniRule annotation

Cofactori

Note: Binds 2 metal cations per subunit. The catalytic dinuclear metal-binding site could be either a di-iron or a manganese-iron cofactor.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Iron 1UniRule annotation1 Publication1
Metal bindingi73Iron 1UniRule annotation1 Publication1
Metal bindingi73Iron 2UniRule annotation1 Publication1
Metal bindingi76Iron 1; via pros nitrogenUniRule annotation1 Publication1
Metal bindingi128Iron 2UniRule annotation1 Publication1
Metal bindingi160Iron 2; via pros nitrogenUniRule annotation1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17306.
BRENDAi4.1.99.5. 5023.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde decarbonylaseUniRule annotation (EC:4.1.99.5UniRule annotation)
Short name:
ADUniRule annotation
Alternative name(s):
Fatty aldehyde decarbonylaseUniRule annotation
Gene namesi
Ordered Locus Names:PMT_1231
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001423 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004189041 – 243Aldehyde decarbonylaseAdd BLAST243

Interactioni

Protein-protein interaction databases

STRINGi74547.PMT1231.

Structurei

Secondary structure

1243
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi28 – 58Combined sources31
Helixi60 – 62Combined sources3
Helixi63 – 86Combined sources24
Helixi93 – 112Combined sources20
Helixi116 – 123Combined sources8
Helixi126 – 138Combined sources13
Helixi139 – 141Combined sources3
Helixi144 – 203Combined sources60
Helixi208 – 226Combined sources19
Helixi230 – 237Combined sources8
Helixi238 – 241Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OC5X-ray1.68A1-243[»]
4KVQX-ray1.84A1-243[»]
4KVRX-ray1.88A1-243[»]
4KVSX-ray1.67A1-243[»]
4PG0X-ray1.90A1-243[»]
4PG1X-ray1.70A2-243[»]
4PGIX-ray2.08A1-243[»]
4PGKX-ray2.17A1-243[»]
4TW3X-ray1.60A21-243[»]
ProteinModelPortaliQ7V6D4.
SMRiQ7V6D4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7V6D4.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde decarbonylase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG410612X. Bacteria.
ENOG410Y0RU. LUCA.
KOiK14331.
OMAiGEQEAHD.
OrthoDBiPOG091H15AL.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
HAMAPiMF_00931. Aldeh_decarbonylase. 1 hit.
InterProiIPR022612. Ald_deCOase.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
[Graphical view]
PfamiPF11266. Ald_deCOase. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR04059. Ald_deCOase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7V6D4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTLEMPVAA VLDSTVGSSE ALPDFTSDRY KDAYSRINAI VIEGEQEAHD
60 70 80 90 100
NYIAIGTLLP DHVEELKRLA KMEMRHKKGF TACGKNLGVE ADMDFAREFF
110 120 130 140 150
APLRDNFQTA LGQGKTPTCL LIQALLIEAF AISAYHTYIP VSDPFARKIT
160 170 180 190 200
EGVVKDEYTH LNYGEAWLKA NLESCREELL EANRENLPLI RRMLDQVAGD
210 220 230 240
AAVLQMDKED LIEDFLIAYQ ESLTEIGFNT REITRMAAAA LVS
Length:243
Mass (Da):27,179
Last modified:October 1, 2003 - v1
Checksum:iAFCB3E58ED4441E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE21406.1.
RefSeqiWP_011130600.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE21406; CAE21406; PMT_1231.
KEGGipmt:PMT_1231.
PATRICi23010881. VBIProMar135351_1589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548175 Genomic DNA. Translation: CAE21406.1.
RefSeqiWP_011130600.1. NC_005071.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OC5X-ray1.68A1-243[»]
4KVQX-ray1.84A1-243[»]
4KVRX-ray1.88A1-243[»]
4KVSX-ray1.67A1-243[»]
4PG0X-ray1.90A1-243[»]
4PG1X-ray1.70A2-243[»]
4PGIX-ray2.08A1-243[»]
4PGKX-ray2.17A1-243[»]
4TW3X-ray1.60A21-243[»]
ProteinModelPortaliQ7V6D4.
SMRiQ7V6D4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi74547.PMT1231.

Protocols and materials databases

DNASUi1728804.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE21406; CAE21406; PMT_1231.
KEGGipmt:PMT_1231.
PATRICi23010881. VBIProMar135351_1589.

Phylogenomic databases

eggNOGiENOG410612X. Bacteria.
ENOG410Y0RU. LUCA.
KOiK14331.
OMAiGEQEAHD.
OrthoDBiPOG091H15AL.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17306.
BRENDAi4.1.99.5. 5023.

Miscellaneous databases

EvolutionaryTraceiQ7V6D4.

Family and domain databases

Gene3Di1.20.1260.10. 1 hit.
HAMAPiMF_00931. Aldeh_decarbonylase. 1 hit.
InterProiIPR022612. Ald_deCOase.
IPR009078. Ferritin-like_SF.
IPR012347. Ferritin-rel.
[Graphical view]
PfamiPF11266. Ald_deCOase. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
TIGRFAMsiTIGR04059. Ald_deCOase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiALDEC_PROMM
AccessioniPrimary (citable) accession number: Q7V6D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.