ID B4DDM5_HUMAN Unreviewed; 717 AA.
AC B4DDM5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 13-SEP-2023, entry version 66.
DE SubName: Full=cDNA FLJ53298, highly similar to Peroxisomal multifunctional enzyme type 2 {ECO:0000313|EMBL:BAG56786.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG56786.1};
RN [1] {ECO:0000313|EMBL:BAG56786.1}
RP NUCLEOTIDE SEQUENCE.
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) 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}.
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DR EMBL; AK293254; BAG56786.1; -; mRNA.
DR AlphaFoldDB; B4DDM5; -.
DR PeptideAtlas; B4DDM5; -.
DR UniPathway; UPA00659; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd03448; HDE_HSD; 1.
DR CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
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; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR13078:SF56; PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2; 1.
DR PANTHER; PTHR13078; PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 465..581
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT DOMAIN 609..712
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
SQ SEQUENCE 717 AA; 77428 MW; 453D578F1B81CBA9 CRC64;
MGSPLRFDGR VVLVTGAGAG LGRAYALAFA ERGALVVVND LGGDFKGVGK GSLAADKVVE
EIRRRGGKAV ANYDSVEEGE KVVKTALDAF GRIDVVVNNA GILRDRSFAR ISDEDWEHMK
KQKYGRIIMT SSASGIYGNF GQANYSAAKL GLLGLANSLA IEGRKSNIHC NTIAPNAGSR
MTQTVMPEDL VEALKPEYVA PLVLWLCHES CEENGGLFEV GAGWIGKLRW ERTLGAIVRQ
KNHPMTPEAV KANWKKICDF ENASKPQSIQ ESSGSIIEVL SKIDSEGGVS ANHTSRATST
ATSGFAGAIG QKLPPFSYAY TELEAIMYAL GVGASIKDPK DLKFIYEGSS DFSCLPTFGV
IIGQKSMMGG GLAEIPGLSI NFAKVLHGEQ YLELYKPLPR AGKLKCEAVV ADVLDKGSGV
VIIMDVYSYS EKELICHNQF SLFLVGSGGF GGKRTSDKVK VAVAIPNRPP DAVLTDTTSL
NQAALYRLSG DWNPLHIDPN FASLAGFDKP ILHGLCTFGF SARRVLQQFA DNDVSRFKAI
KARFAKPVYP GQTLQTEMWK EGNRIHFQTK VQETGDIVIS NAYVDLAPTS GTSAKTPSEG
GKLQSTFVFE EIGRRLKDIG PEVVKKVNAV FEWHITKGGN IGAKWTIDLK SGSGKVYQGP
AKGAADTTII LSDEDFMEVV LGKLDPQKAF FSGRLKARGN IMLSQKLQMI LKDYAKL
//