ID W1QFR2_OGAPD Unreviewed; 915 AA.
AC W1QFR2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Multifunctional enzyme of the peroxisomal fatty acid beta-oxidation pathway {ECO:0000313|EMBL:ESX00902.1};
DE EC=4.2.1.119 {ECO:0000313|EMBL:ESX00902.1};
GN ORFNames=HPODL_00315 {ECO:0000313|EMBL:ESX00902.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESX00902.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESX00902.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:ESX00902.1}.
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DR EMBL; AEOI02000005; ESX00902.1; -; Genomic_DNA.
DR RefSeq; XP_013935736.1; XM_014080261.1.
DR AlphaFoldDB; W1QFR2; -.
DR STRING; 871575.W1QFR2; -.
DR GeneID; 25769788; -.
DR KEGG; opa:HPODL_00315; -.
DR eggNOG; KOG1206; Eukaryota.
DR HOGENOM; CLU_010194_18_1_1; -.
DR OMA; WATKVHT; -.
DR OrthoDB; 2140828at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008673; Chromosome III.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00106; adh_short; 2.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR PROSITE; PS00061; ADH_SHORT; 2.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000313|EMBL:ESX00902.1}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673}.
FT DOMAIN 796..899
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT REGION 608..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..631
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 100580 MW; 3D82671B0B12074C CRC64;
MRQQKYISCH APLCFFMGEI ELKDLVVIIT GAGGGLGRQY ALSFASRGAK VVVNDLGGTL
GGSGTSTKAA DVVVDEIRKD GGTAVANYDN VVTNPDGIVR TAVEAFGTVH VLINNAGILK
DAAFKNMTEK QFLDVLDVHL NGAFKLTKLC WPLFRQQKFG RIIMTTSPAG LYGNFGQTNY
SAAKMGLVGL AETLAKEGAK YNIKANAIAP LAKSRMTETV MPPDVLKKLL PEKVAPLVLY
LSSRGCNCSG CIFEVAAGLF AQIRWERSGG LLLKPDESLT PEAILSKFSQ VTDFTNAQYP
TQLNDYNSLL EQAKKLPPND QGSTRISSLK DKVVIITGAG SGLGRHHALW FARYGAKVVV
NDFQDPSGVV DEIRQAGGTA VGARFNVYSD ADKIVKTALD AFGTVNVLVN NAGILRDRSF
AKMSQQEWDH VIQIHLVATF RLCKLVWPIF LEQKGGSIIN TTSTSGIYGN FGQANYAAAK
AAVLSFTRSL SLEGAKANIR CNAIAPHAET SMTKTIFKSD ELNKFSADQV SPLVVLLASD
ELKVSGELYE VGAGWVGNTR WQRAIGAVSH DDYIAPEFIE QHWAEITDFS KGVNMKSAQQ
SAMAILESVG GKDEDEDEED EEEEDEEDED SSVKTDGYRY DHRQVILYNL SVGCHAEELK
YVYENDDDFQ AVPTFGVIPF LNEGSDSFDF SDLVKNFDMT KLLHGEHYLK IAKQIPTSGK
LKTKSFPVAV FNKHKNGKKN SLVIEGYETH DEKGELVFYN QGSYFIRNSE TASGKDEVFN
KRSIPFLQNS FEARGRPDFE STYTTFSDQA ALYRLNGDFN PLHIDPVFAR GGNFSRPILH
GLGTMGISAK LLMDHYGVFD EIKVRFTNVV YPGEQLKVLG WKSGQTVVFQ TWSVDRNCLV
IDRAGIRLKE TKSKL
//
