ALDEC_SYNY3
ID ALDEC_SYNY3 Reviewed; 231 AA.
AC Q55688;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=sll0208;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 -!- DISRUPTION PHENOTYPE: Abolishes the presence of alkanes.
CC {ECO:0000269|PubMed:20671186}.
CC -!- SIMILARITY: Belongs to the aldehyde decarbonylase family.
CC {ECO:0000255|HAMAP-Rule:MF_00931}.
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DR EMBL; BA000022; BAA10217.1; -; Genomic_DNA.
DR PIR; S76365; S76365.
DR PDB; 4Z5S; X-ray; 1.58 A; A=1-231.
DR PDBsum; 4Z5S; -.
DR AlphaFoldDB; Q55688; -.
DR SMR; Q55688; -.
DR IntAct; Q55688; 7.
DR STRING; 1148.1001589; -.
DR PaxDb; Q55688; -.
DR EnsemblBacteria; BAA10217; BAA10217; BAA10217.
DR KEGG; syn:sll0208; -.
DR eggNOG; COG1633; Bacteria.
DR InParanoid; Q55688; -.
DR OMA; GEQEAHD; -.
DR BRENDA; 4.1.99.5; 6192.
DR Proteomes; UP000001425; Chromosome.
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; Reference proteome.
FT CHAIN 1..231
FT /note="Aldehyde decarbonylase"
FT /id="PRO_0000418905"
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 HELIX 15..45
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 50..73
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 80..99
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 159..190
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 195..213
FT /evidence="ECO:0007829|PDB:4Z5S"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:4Z5S"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4Z5S"
SQ SEQUENCE 231 AA; 26178 MW; 729215496B3D5BC9 CRC64;
MPELAVRTEF DYSSEIYKDA YSRINAIVIE GEQEAYSNYL QMAELLPEDK EELTRLAKME
NRHKKGFQAC GNNLQVNPDM PYAQEFFAGL HGNFQHAFSE GKVVTCLLIQ ALIIEAFAIA
AYNIYIPVAD DFARKITEGV VKDEYTHLNY GEEWLKANFA TAKEELEQAN KENLPLVWKM
LNQVQGDAKV LGMEKEALVE DFMISYGEAL SNIGFSTREI MRMSSYGLAG V
