ALDEC_PROMM
ID ALDEC_PROMM Reviewed; 243 AA.
AC Q7V6D4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PMT_1231;
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
RN [2]
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH IRON.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of hypothetical protein (NP_895059.1) from
RT Prochlorococcus marinus MIT9313 at 1.68 A resolution.";
RL Submitted (DEC-2006) to the PDB data bank.
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 -!- SIMILARITY: Belongs to the aldehyde decarbonylase family.
CC {ECO:0000255|HAMAP-Rule:MF_00931}.
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DR EMBL; BX548175; CAE21406.1; -; Genomic_DNA.
DR RefSeq; WP_011130600.1; NC_005071.1.
DR PDB; 2OC5; X-ray; 1.68 A; A=1-243.
DR PDB; 4KVQ; X-ray; 1.84 A; A=1-243.
DR PDB; 4KVR; X-ray; 1.88 A; A=1-243.
DR PDB; 4KVS; X-ray; 1.67 A; A=1-243.
DR PDB; 4PG0; X-ray; 1.90 A; A=1-243.
DR PDB; 4PG1; X-ray; 1.70 A; A=2-243.
DR PDB; 4PGI; X-ray; 2.08 A; A=1-243.
DR PDB; 4PGK; X-ray; 2.17 A; A=1-243.
DR PDB; 4TW3; X-ray; 1.60 A; A=21-243.
DR PDBsum; 2OC5; -.
DR PDBsum; 4KVQ; -.
DR PDBsum; 4KVR; -.
DR PDBsum; 4KVS; -.
DR PDBsum; 4PG0; -.
DR PDBsum; 4PG1; -.
DR PDBsum; 4PGI; -.
DR PDBsum; 4PGK; -.
DR PDBsum; 4TW3; -.
DR AlphaFoldDB; Q7V6D4; -.
DR SMR; Q7V6D4; -.
DR STRING; 74547.PMT_1231; -.
DR PRIDE; Q7V6D4; -.
DR DNASU; 1728804; -.
DR EnsemblBacteria; CAE21406; CAE21406; PMT_1231.
DR KEGG; pmt:PMT_1231; -.
DR eggNOG; COG3396; Bacteria.
DR HOGENOM; CLU_1106729_0_0_3; -.
DR OMA; GEQEAHD; -.
DR OrthoDB; 924133at2; -.
DR BioCyc; MetaCyc:MON-17306; -.
DR BRENDA; 4.1.99.5; 5023.
DR EvolutionaryTrace; Q7V6D4; -.
DR Proteomes; UP000001423; 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..243
FT /note="Aldehyde decarbonylase"
FT /id="PRO_0000418904"
FT BINDING 45
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931,
FT ECO:0000269|Ref.3"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931,
FT ECO:0000269|Ref.3"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931,
FT ECO:0000269|Ref.3"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931,
FT ECO:0000269|Ref.3"
FT BINDING 128
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931,
FT ECO:0000269|Ref.3"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00931,
FT ECO:0000269|Ref.3"
FT HELIX 28..58
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 63..86
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 93..112
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 144..203
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 208..226
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:4TW3"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4TW3"
SQ SEQUENCE 243 AA; 27179 MW; AFCB3E58ED4441E1 CRC64;
MPTLEMPVAA VLDSTVGSSE ALPDFTSDRY KDAYSRINAI VIEGEQEAHD NYIAIGTLLP
DHVEELKRLA KMEMRHKKGF TACGKNLGVE ADMDFAREFF APLRDNFQTA LGQGKTPTCL
LIQALLIEAF AISAYHTYIP VSDPFARKIT EGVVKDEYTH LNYGEAWLKA NLESCREELL
EANRENLPLI RRMLDQVAGD AAVLQMDKED LIEDFLIAYQ ESLTEIGFNT REITRMAAAA
LVS
