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Database: UniProt
Entry: M3HDV7_CANMX
LinkDB: M3HDV7_CANMX
Original site: M3HDV7_CANMX 
ID   M3HDV7_CANMX            Unreviewed;      1301 AA.
AC   M3HDV7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Fatty acid synthase beta subunit dehydratase {ECO:0000313|EMBL:EMG45417.1};
DE   Flags: Fragment;
GN   ORFNames=G210_4400 {ECO:0000313|EMBL:EMG45417.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG45417.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG45417.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG45417.1}.
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DR   EMBL; AOGT01002478; EMG45417.1; -; Genomic_DNA.
DR   STRING; 1245528.M3HDV7; -.
DR   eggNOG; ENOG502QQJX; Eukaryota.
DR   HOGENOM; CLU_000114_5_1_1; -.
DR   OMA; HDGHIAR; -.
DR   OrthoDB; 5488314at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR   GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR   GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd03447; FAS_MaoC; 1.
DR   Gene3D; 1.20.930.70; -; 1.
DR   Gene3D; 3.30.1120.100; -; 1.
DR   Gene3D; 3.30.70.3330; -; 1.
DR   Gene3D; 6.10.140.1400; -; 1.
DR   Gene3D; 6.10.60.10; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013565; Fas1/AflB-like_central.
DR   InterPro; IPR040883; FAS_meander.
DR   InterPro; IPR003965; Fatty_acid_synthase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR039569; MaoC-like_dehydrat_N.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR   Pfam; PF17951; FAS_meander; 1.
DR   Pfam; PF13452; MaoC_dehydrat_N; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   PRINTS; PR01483; FASYNTHASE.
DR   SMART; SM00827; PKS_AT; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT   DOMAIN          916..1270
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000259|SMART:SM00827"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMG45417.1"
SQ   SEQUENCE   1301 AA;  146453 MW;  9A885DAB9FF7F2C0 CRC64;
     MYSKIRRCSN IILVAGSGFG SDEDTYPYLT GLWSKKFNYP PMPFDGVLFG SRVMTAKEAH
     TSLEAKKLIA QCPGVPDEKW EQTYKKPTGG IITVRSEMGE PIHKIATRGV MFWKELDETI
     FNLPKNKLLE GLNKKRDYII KKLNNDFQKP WFAKNANGVC DLQEMTYEEI ANRLVELMYV
     KKSQRWIDVS LRNLYGDYLR RVEERFTSQT GVVSLLQNFG QLSEPEKFTA EFFKKFPAAK
     QQLISQEDAD HFLLLAARPA QKPVPFVPVL DERFEFFFKK DSLWQSEDLE SVVGEDVQRT
     CILHGPVASQ FTNKVDEPIG EILDSIHDGH IARLIKDEYA GDESKIPVVE YFGGYNAREV
     AVAAENVEIT DSKQEVVYEI GTKLPAKQDW LDLLAGTELN WLHALLATDR IVQGTRHVAN
     SLHDILTPVP HSKVVINKST QKLTAYEKVK GELLPVAEIE LIKPNTIQLS LIEHRTADGK
     PVALPFLYNY NPADGFAPIL EVMGDRNDRI KEFYWKLWFG SSVPYDNEIN VEEQILGEEI
     TISSQDISEF THAIGNKCEA FVNRPGKVTL APMDFAIVIG WKAIIKAIFP KTVDGDLLKL
     VHLSNGYKMI TGAKPLQKDD VVSTKAEIRA VLNQPSGKLV EVVGTIYREG KPVMEVTSQF
     LYRGEYNDYN NTFQKVTETP YKVAFNAPKD LAVLRSKEWF HLEKDVEFDA LTFRCESTYK
     FKSANVYSSI RTTGQVLLEL PTQEVIQIGT VDYEAGTSYG NPVTDYLSRN GKTIEEAVTF
     ENAIPLSSGE ELTSKAPGTN EPYAIVSGDY NPIHVSRVFA AYAKLPGTIT HGMYSSASIR
     GLVEEWAANN VAARVRAFKC DFVGMVLPND TLQTTMEHVG MINGRKIIKV ETRNVETEVP
     VLIAEAEIEQ PTTTYVFTGQ GSQEQGMGMD LYNSSEVARA VWDKADKHFI NNYGFSILDI
     VQNNPKEMTI HFGGAKGRAI RDNYITMMFE TIGEDGSLKS EKIFKDIDET TTSYTFVSDT
     GLLSATQFTQ PALTLMEKAA YEDIKSKGLI PTDIMFAGHS LGEYSALSSL ANVMPIESLV
     DVVFYRGMTM QVAVARDEYG RSNYGMVAVN PTRVSPTFND AALRFVVDEV SNKTTWLLEI
     VNYNVENQQY VAAGDLRALD TLTNVLNVLK INKIDIVKLQ EQLSIEKVKE HLYEIIDEVA
     AKSLAKPQPI DLERGFAVIP LKGISVPFHS SYLMSGVKPF KRFLCKKIPK SSVKPQDLIG
     KYIPNLTAKP FELTKEYFQD VYDLTKSEKI KNILDNWEKY E
//
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