ALDEC_NOSP7
ID ALDEC_NOSP7 Reviewed; 232 AA.
AC B2J1M1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Npun_R1711;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, MUTAGENESIS OF TYR-123, AND COFACTOR.
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).
RN [3]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=21341652; DOI=10.1021/ja111607x;
RA Warui D.M., Li N., Norgaard H., Krebs C., Bollinger J.M. Jr., Booker S.J.;
RT "Detection of formate, rather than carbon monoxide, as the stoichiometric
RT coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial
RT aldehyde decarbonylase.";
RL J. Am. Chem. Soc. 133:3316-3319(2011).
CC -!- FUNCTION: Catalyzes the decarbonylation of fatty aldehydes to alkanes.
CC Involved in the biosynthesis of alkanes, mainly heptadecane and
CC pentadecane. Requires the presence of ferredoxin, ferredoxin reductase
CC and NADPH for in vitro decarbonylase activity. {ECO:0000255|HAMAP-
CC 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 ECO:0000269|PubMed:21341652};
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, ECO:0000269|PubMed:20671186,
CC ECO:0000269|PubMed:21341652};
CC -!- SIMILARITY: Belongs to the aldehyde decarbonylase family.
CC {ECO:0000255|HAMAP-Rule:MF_00931}.
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DR EMBL; CP001037; ACC80382.1; -; Genomic_DNA.
DR RefSeq; WP_012408400.1; NC_010628.1.
DR PDB; 5UXI; X-ray; 2.00 A; A=1-232.
DR PDBsum; 5UXI; -.
DR AlphaFoldDB; B2J1M1; -.
DR SMR; B2J1M1; -.
DR STRING; 63737.Npun_R1711; -.
DR EnsemblBacteria; ACC80382; ACC80382; Npun_R1711.
DR KEGG; npu:Npun_R1711; -.
DR eggNOG; COG1633; Bacteria.
DR HOGENOM; CLU_1106729_0_0_3; -.
DR OMA; GEQEAHD; -.
DR OrthoDB; 924133at2; -.
DR PhylomeDB; B2J1M1; -.
DR BioCyc; MetaCyc:MON-17309; -.
DR BRENDA; 4.1.99.5; 4370.
DR Proteomes; UP000001191; 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..232
FT /note="Aldehyde decarbonylase"
FT /id="PRO_0000418903"
FT BINDING 33
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 61
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931"
FT MUTAGEN 123
FT /note="Y->F: No detectable effect on alkane biosynthesis
FT activity in vivo."
FT /evidence="ECO:0000269|PubMed:20671186"
FT HELIX 16..46
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 51..74
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 81..100
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 160..184
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 196..214
FT /evidence="ECO:0007829|PDB:5UXI"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:5UXI"
SQ SEQUENCE 232 AA; 26304 MW; A5AEE61EAE272F67 CRC64;
MQQLTDQSKE LDFKSETYKD AYSRINAIVI EGEQEAHENY ITLAQLLPES HDELIRLSKM
ESRHKKGFEA CGRNLAVTPD LQFAKEFFSG LHQNFQTAAA EGKVVTCLLI QSLIIECFAI
AAYNIYIPVA DDFARKITEG VVKEEYSHLN FGEVWLKEHF AESKAELELA NRQNLPIVWK
MLNQVEGDAH TMAMEKDALV EDFMIQYGEA LSNIGFSTRD IMRLSAYGLI GA
