ID   CERR_CAUVN              Reviewed;         317 AA.
AC   A0A0H3C8X7;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Ceramide reductase {ECO:0000303|PubMed:34969973};
DE            EC=1.-.-.- {ECO:0000305|PubMed:34969973};
DE   Flags: Precursor;
GN   Name=cerR {ECO:0000303|PubMed:34969973};
GN   OrderedLocusNames=CCNA_01222 {ECO:0000312|EMBL:ACL94687.1};
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=33063925; DOI=10.1111/1462-2920.15280;
RA   Olea-Ozuna R.J., Poggio S., Bergstroem E., Quiroz-Rocha E.,
RA   Garcia-Soriano D.A., Sahonero-Canavesi D.X., Padilla-Gomez J.,
RA   Martinez-Aguilar L., Lopez-Lara I.M., Thomas-Oates J., Geiger O.;
RT   "Five structural genes required for ceramide synthesis in Caulobacter and
RT   for bacterial survival.";
RL   Environ. Microbiol. 23:143-159(2021).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=34969973; DOI=10.1038/s41589-021-00948-7;
RA   Stankeviciute G., Tang P., Ashley B., Chamberlain J.D., Hansen M.E.B.,
RA   Coleman A., D'Emilia R., Fu L., Mohan E.C., Nguyen H., Guan Z.,
RA   Campopiano D.J., Klein E.A.;
RT   "Convergent evolution of bacterial ceramide synthesis.";
RL   Nat. Chem. Biol. 18:305-312(2022).
CC   -!- FUNCTION: Involved in de novo bacterial ceramide synthesis
CC       (PubMed:33063925, PubMed:34969973). Catalyzes the reduction of
CC       bacterial oxidized ceramides to bacterial dihydroceramides
CC       (PubMed:34969973). {ECO:0000269|PubMed:33063925,
CC       ECO:0000269|PubMed:34969973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N-acyl-3-oxosphinganine + NADH = an N-acylsphinganine +
CC         NAD(+); Xref=Rhea:RHEA:70527, ChEBI:CHEBI:15378, ChEBI:CHEBI:31488,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:189535;
CC         Evidence={ECO:0000269|PubMed:34969973};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70528;
CC         Evidence={ECO:0000269|PubMed:34969973};
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:34969973}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant cannot form dihydroceramide
CC       (PubMed:33063925). Deletion of the gene results in a ceramide molecule
CC       with a mass reduction of 2 Da, corresponding to a loss of two hydrogens
CC       (PubMed:34969973). Mutants are impaired in growth at elevated
CC       temperatures but are resistant towards the antibiotic polymyxin B
CC       (PubMed:33063925). {ECO:0000269|PubMed:33063925,
CC       ECO:0000269|PubMed:34969973}.
CC   -!- MISCELLANEOUS: The bacterial ceramide synthesis pathway operates in a
CC       different order from that in eukaryotes. Furthermore, phylogenetic
CC       analyses support the hypothesis that the bacterial and eukaryotic
CC       ceramide pathways evolved independently. {ECO:0000269|PubMed:34969973}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; CP001340; ACL94687.1; -; Genomic_DNA.
DR   RefSeq; WP_010919048.1; NC_011916.1.
DR   RefSeq; YP_002516595.1; NC_011916.1.
DR   SMR; A0A0H3C8X7; -.
DR   EnsemblBacteria; ACL94687; ACL94687; CCNA_01222.
DR   GeneID; 7333615; -.
DR   KEGG; ccs:CCNA_01222; -.
DR   PATRIC; fig|565050.3.peg.1204; -.
DR   HOGENOM; CLU_007383_6_1_5; -.
DR   OMA; GFGPKRY; -.
DR   OrthoDB; 1928091at2; -.
DR   PhylomeDB; A0A0H3C8X7; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Lipid metabolism; Oxidoreductase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..317
FT                   /note="Ceramide reductase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000455454"
SQ   SEQUENCE   317 AA;  33857 MW;  AB31F5A268A48816 CRC64;
     MATDARGVVA ITGATGFLGR HLVRALAQDG WRPRVLVRRD PVHPFWRDLE VEVVTGDLGT
     PRALDRLAKG AEVFIHVAGL IKARTLEGFN RVNQDGARAA AEAARAAGAR FILVSSLAAR
     EPSLSNYAAS KRAGEDAVRA ADPSALIVRP PAIYGPGDTE TLGLFQLAAR SPVLPVLSQT
     SRVAMIHVED AAAKLVAFCR TPVLGLVELS DVRRDGYTWT EIMRGAAHVM GAKPRLIRLP
     DPGILTAGAL VDAWSSLTNT PSVFGLGKAR ELLHTDWTPS SAPMAEGVPS KFGLIDGFTH
     TVDWYRAAGW LPKNIVA