ID S7MTA1_MYOBR Unreviewed; 361 AA.
AC S7MTA1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating {ECO:0000313|EMBL:EPQ07694.1};
GN ORFNames=D623_10002609 {ECO:0000313|EMBL:EPQ07694.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07694.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family.
CC {ECO:0000256|ARBA:ARBA00009219, ECO:0000256|RuleBase:RU004475}.
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DR EMBL; KE162284; EPQ07694.1; -; Genomic_DNA.
DR RefSeq; XP_005866186.1; XM_005866124.2.
DR RefSeq; XP_014395098.1; XM_014539612.1.
DR RefSeq; XP_014395099.1; XM_014539613.1.
DR RefSeq; XP_014395100.1; XM_014539614.1.
DR RefSeq; XP_014395101.1; XM_014539615.1.
DR RefSeq; XP_014395102.1; XM_014539616.1.
DR AlphaFoldDB; S7MTA1; -.
DR GeneID; 102257708; -.
DR KEGG; myb:102257708; -.
DR CTD; 50814; -.
DR eggNOG; KOG1430; Eukaryota.
DR OrthoDB; 1133at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1.
DR PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU004475};
KW Oxidoreductase {ECO:0000256|RuleBase:RU004475};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Transmembrane {ECO:0000256|RuleBase:RU004475};
KW Transmembrane helix {ECO:0000256|RuleBase:RU004475}.
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU004475"
FT DOMAIN 30..280
FT /note="3-beta hydroxysteroid dehydrogenase/isomerase"
FT /evidence="ECO:0000259|Pfam:PF01073"
SQ SEQUENCE 361 AA; 40649 MW; 57D3F70FCB6BA4B7 CRC64;
MEQAVGEPKK DQVTGTRLTE DITKAKKCTV IGGSGFLGQH MVEQLLARGY TVNVFDMRQG
FDNPQVQFFL GDLCNQQDLY PALKGVSTVF HCASPPPSSN NKELFYRVNY IGTRNVIETC
KKAEVQKLIL TSSASVIFEG VDIKNGTEDF PYAMKPIDYY TETKILQERE VLGANDPERN
FLTTAIRPHG IFGPRDPQLV PILIEAARKG KMKFMIGNGE NLVDFTFVEN VVHGHILAAE
HLSQDTALGG KAFHITNDEP IPFWTFLSRI LIGLNYEAPK YHIPYWVAYY LALLLSLLVM
VISPVIQLQP TFTPMRVALA GTFHYYSCER AKKALGYQPL VTMDDAVERT VQSFHHLRRV
K
//
