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Database: UniProt
Entry: K8FE99_9CHLO
LinkDB: K8FE99_9CHLO
Original site: K8FE99_9CHLO 
ID   K8FE99_9CHLO            Unreviewed;       528 AA.
AC   K8FE99;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Cytochrome b5 heme-binding domain-containing protein {ECO:0000259|PROSITE:PS50255};
GN   ORFNames=Bathy07g01750 {ECO:0000313|EMBL:CCO66066.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO66066.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO66066.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO66066.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00009295}.
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DR   EMBL; FO082272; CCO66066.1; -; Genomic_DNA.
DR   RefSeq; XP_007511978.1; XM_007511916.1.
DR   AlphaFoldDB; K8FE99; -.
DR   STRING; 41875.K8FE99; -.
DR   GeneID; 19014665; -.
DR   KEGG; bpg:Bathy07g01750; -.
DR   eggNOG; KOG4232; Eukaryota.
DR   OrthoDB; 3715892at2759; -.
DR   Proteomes; UP000198341; Chromosome_7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016717; F:oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water; IEA:UniProt.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProt.
DR   GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IEA:UniProt.
DR   CDD; cd03506; Delta6-FADS-like; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353:SF19; DELTA(5) FATTY ACID DESATURASE C-RELATED; 1.
DR   PANTHER; PTHR19353; FATTY ACID DESATURASE 2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00487; FA_desaturase; 1.
DR   PIRSF; PIRSF015921; FA_sphinglp_des; 1.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198341};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        194..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..112
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   528 AA;  60357 MW;  ADD1192BF0E9E8B0 CRC64;
     MTTTTTTTTT ERKQNLSRSF PSFAKKKSNE TKNDDSNKTS FTRDDVAKHN RSNDCWVIVH
     DRAYDVTKFV PKHPGGNMIH VNAGGECTAL FESYHPLKAR KVLEKFYVGD VVGDEEKEEE
     DERGARRRTT SISTTTTSTK ENKQKSKSEM KAPKYRSNGE EDEFHYECKR AAEKYFKENA
     LDPREHPEMW AKSVAILSGV VLFHYLSFFS ANVAFFPLAC VFAVLHGVCK AEVGVSIQHD
     ANHGAYSKNK KVLHAMQLTL DIVGASSFMW KQQHVVGHHA FTNVEDIDPD IRCDEKNDVR
     RVNYMQPHAF FHKAQHVYLA LMYGLLSFKS CFFDDFSARK NNKIGWVTVP KFERREAVEF
     WGSKAVWAFY YLYLPFKYSP HNDSYAKLFA LWTLTEFTTG WLLAFMFQVA HVTPDVEFFK
     VDEKTGVISS NKSWAEAQLA SSADFAHGSK FWTHFSGGLN YQVIHHLFPG VCHVHYPQLA
     PLVMDVCKKR GLEYVVYPTF WAALRAHFRH LKNVGGGAFK VPSLHTVG
//
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