ALDEC_SYNE7
ID ALDEC_SYNE7 Reviewed; 231 AA.
AC Q54764;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Aldehyde decarbonylase {ECO:0000255|HAMAP-Rule:MF_00931};
DE Short=AD {ECO:0000255|HAMAP-Rule:MF_00931};
DE EC=4.1.99.5 {ECO:0000255|HAMAP-Rule:MF_00931};
DE AltName: Full=Fatty aldehyde decarbonylase {ECO:0000255|HAMAP-Rule:MF_00931};
GN OrderedLocusNames=Synpcc7942_1593;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RA Phung L.T., Haselkorn R.;
RT "Genes encoding the alpha subunit of carboxyltransferase of the acetyl-CoA
RT carboxylase complex and GTP cyclohydrolase I from cyanobacterium
RT Synechococcus sp. PCC 7942.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=20671186; DOI=10.1126/science.1187936;
RA Schirmer A., Rude M.A., Li X., Popova E., del Cardayre S.B.;
RT "Microbial biosynthesis of alkanes.";
RL Science 329:559-562(2010).
CC -!- FUNCTION: Catalyzes the decarbonylation of fatty aldehydes to alkanes.
CC Requires the presence of ferredoxin, ferredoxin reductase and NADPH for
CC in vitro decarbonylase activity (By similarity). Involved in the
CC biosynthesis of alkanes, mainly heptadecane and pentadecane.
CC {ECO:0000255|HAMAP-Rule:MF_00931, ECO:0000269|PubMed:20671186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-
CC chain alkane + formate + H2O + 2 NADP(+); Xref=Rhea:RHEA:21440,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17176, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83563; EC=4.1.99.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00931};
CC -!- COFACTOR:
CC Note=Binds 2 metal cations per subunit. The catalytic dinuclear metal-
CC binding site could be either a di-iron or a manganese-iron cofactor.
CC {ECO:0000255|HAMAP-Rule:MF_00931};
CC -!- SIMILARITY: Belongs to the aldehyde decarbonylase family.
CC {ECO:0000255|HAMAP-Rule:MF_00931}.
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DR EMBL; U59236; AAB82038.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57623.1; -; Genomic_DNA.
DR RefSeq; WP_011378104.1; NC_007604.1.
DR PDB; 4QUW; X-ray; 2.26 A; A=1-231.
DR PDB; 4RC5; X-ray; 2.30 A; A=11-231, B=10-231.
DR PDB; 4RC6; X-ray; 2.90 A; A=13-227, B=16-227.
DR PDB; 4RC7; X-ray; 2.20 A; A=11-230, B=10-231.
DR PDB; 4RC8; X-ray; 1.71 A; A/B=10-231.
DR PDBsum; 4QUW; -.
DR PDBsum; 4RC5; -.
DR PDBsum; 4RC6; -.
DR PDBsum; 4RC7; -.
DR PDBsum; 4RC8; -.
DR AlphaFoldDB; Q54764; -.
DR SMR; Q54764; -.
DR STRING; 1140.Synpcc7942_1593; -.
DR PRIDE; Q54764; -.
DR EnsemblBacteria; ABB57623; ABB57623; Synpcc7942_1593.
DR KEGG; syf:Synpcc7942_1593; -.
DR eggNOG; COG1633; Bacteria.
DR HOGENOM; CLU_1106729_0_0_3; -.
DR OMA; GEQEAHD; -.
DR OrthoDB; 924133at2; -.
DR BioCyc; MetaCyc:SYNPCC7942_1593-MON; -.
DR BioCyc; SYNEL:SYNPCC7942_1593-MON; -.
DR BRENDA; 4.1.99.5; 7781.
DR GO; GO:0071771; F:aldehyde decarbonylase activity; IMP:CACAO.
DR GO; GO:1990465; F:aldehyde oxygenase (deformylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009924; F:octadecanal decarbonylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1260.10; -; 1.
DR HAMAP; MF_00931; Aldeh_decarbonylase; 1.
DR InterPro; IPR022612; Ald_deCOase.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR Pfam; PF11266; Ald_deCOase; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR TIGRFAMs; TIGR04059; Ald_deCOase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Lyase; Metal-binding; NADP.
FT CHAIN 1..231
FT /note="Aldehyde decarbonylase"
FT /id="PRO_0000418902"
FT BINDING 32
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 115
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4QUW"
FT HELIX 15..45
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 50..73
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 80..99
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 131..157
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 159..190
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 195..213
FT /evidence="ECO:0007829|PDB:4RC8"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:4RC8"
SQ SEQUENCE 231 AA; 26369 MW; 7168C8103A1D0951 CRC64;
MPQLEASLEL DFQSESYKDA YSRINAIVIE GEQEAFDNYN RLAEMLPDQR DELHKLAKME
QRHMKGFMAC GKNLSVTPDM GFAQKFFERL HENFKAAAAE GKVVTCLLIQ SLIIECFAIA
AYNIYIPVAD AFARKITEGV VRDEYLHRNF GEEWLKANFD ASKAELEEAN RQNLPLVWLM
LNEVADDARE LGMERESLVE DFMIAYGEAL ENIGFTTREI MRMSAYGLAA V
