ID   CERH_CAUVN              Reviewed;         351 AA.
AC   A0A0H3C677;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Ceramide hydroxylase {ECO:0000303|PubMed:34969973};
GN   Name=cerH {ECO:0000303|PubMed:34969973};
GN   OrderedLocusNames=CCNA_00202 {ECO:0000312|EMBL:ACL93669.1};
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=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       {ECO:0000269|PubMed:34969973}.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to a ceramide molecule
CC       with a mass reduction of 16 Da corresponding to the loss of a hydroxyl
CC       group. {ECO:0000269|PubMed:34969973}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CP001340; ACL93669.1; -; Genomic_DNA.
DR   RefSeq; WP_012639906.1; NC_011916.1.
DR   RefSeq; YP_002515577.1; NC_011916.1.
DR   EnsemblBacteria; ACL93669; ACL93669; CCNA_00202.
DR   GeneID; 7330248; -.
DR   KEGG; ccs:CCNA_00202; -.
DR   PATRIC; fig|565050.3.peg.200; -.
DR   HOGENOM; CLU_780549_0_0_5; -.
DR   OMA; PYHNLGK; -.
DR   OrthoDB; 1032884at2; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   Pfam; PF00487; FA_desaturase; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Lipid metabolism; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..351
FT                   /note="Ceramide hydroxylase"
FT                   /id="PRO_0000455457"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   351 AA;  38920 MW;  9981ABB33698B853 CRC64;
     MAKTASDISL TRQAMSLTED LMTPNAAIYW ADLTISAAVM WGGFLIAATT SSLALGLGAA
     LLSMLALYRG LSFIHELTHI RDDEAPGFRV GWNVLVGVPL MTPSLMYEGV HNIHHIKDRF
     GTRLDPEYLP LSRFTPLKLA GFLFIALLAP LGVILRSAIL IPLSFLVPSL RRYLKTKLSA
     LIINPDFVRE DLGRWRKAWV IQDVACWLWS WAVIAGLGLG VVPVRVVLTG LAIFSLATFL
     NQARTLVAHH WDNDGDKMTL EEQFLDSVNV PPPNLASALW APVGLRYHAL HHLLPRLPYH
     NMAKAHARLV EALGADSLYH RASEPGLFEA LGDLFRRVRQ KNAEARNQPA H