ID   ACR1_ACIAD              Reviewed;         295 AA.
AC   Q6F7B8; P94129;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Fatty acyl-CoA reductase;
DE            EC=1.2.1.n2;
GN   Name=acr1; OrderedLocusNames=ACIAD3383;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=9139916; DOI=10.1128/jb.179.9.2969-2975.1997;
RA   Reiser S., Somerville C.;
RT   "Isolation of mutants of Acinetobacter calcoaceticus deficient in wax ester
RT   synthesis and complementation of one mutation with a gene encoding a fatty
RT   acyl coenzyme A reductase.";
RL   J. Bacteriol. 179:2969-2975(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of long chain acyl-
CC       CoA (with chain lengths of 14 to 22 carbons) to the corresponding
CC       aldehyde. {ECO:0000269|PubMed:9139916}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + hexadecanal + NADP(+) = H(+) + hexadecanoyl-CoA + NADPH;
CC         Xref=Rhea:RHEA:27270, ChEBI:CHEBI:15378, ChEBI:CHEBI:17600,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.n2;
CC         Evidence={ECO:0000269|PubMed:9139916};
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG70047.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U77680; AAC45217.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG70047.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004923651.1; NC_005966.1.
DR   AlphaFoldDB; Q6F7B8; -.
DR   SMR; Q6F7B8; -.
DR   STRING; 62977.ACIAD3383; -.
DR   PRIDE; Q6F7B8; -.
DR   EnsemblBacteria; CAG70047; CAG70047; ACIAD3383.
DR   GeneID; 45235577; -.
DR   KEGG; aci:ACIAD3383; -.
DR   eggNOG; COG4221; Bacteria.
DR   HOGENOM; CLU_010194_2_1_6; -.
DR   OrthoDB; 1582456at2; -.
DR   BioCyc; ASP62977:ACIAD_RS15310-MON; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Lipid metabolism; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..295
FT                   /note="Fatty acyl-CoA reductase"
FT                   /id="PRO_0000382695"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         21..28
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        234
FT                   /note="K -> T (in Ref. 1; AAC45217)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   295 AA;  32529 MW;  A81F1A7B9FC4B34D CRC64;
     MNKKLEALFR ENVKGKVALI TGASSGIGLT IAKRIAAAGA HVLLVARTQE TLEEVKAAIE
     QQGGQASIFP CDLTDMNAID QLSQQIMASV DHVDFLINNA GRSIRRAVHE SFDRFHDFER
     TMQLNYFGAV RLVLNLLPHM IKRKNGQIIN ISSIGVLANA TRFSAYVASK AALDAFSRCL
     SAEVLKHKIS ITSIYMPLVR TPMIAPTKIY KYVPTLSPEE AADLIVYAIV KRPKRIATHL
     GRLASITYAI APDINNILMS IGFNLFPSST AALGEQEKLN LLQRAYARLF PGEHW