CHSH2_THECD
ID CHSH2_THECD Reviewed; 319 AA.
AC D1AB77;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Probable enoyl-CoA hydratase alpha subunit {ECO:0000305};
DE EC=4.2.1.- {ECO:0000250|UniProtKB:I6YGF8};
GN Name=chsH2 {ECO:0000303|PubMed:31209106};
GN OrderedLocusNames=Tcur_3482 {ECO:0000312|EMBL:ACY99020.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC Thermomonospora.
OX NCBI_TaxID=471852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goeker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
RN [2] {ECO:0007744|PDB:6OK1}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 188-319 IN COMPLEX WITH LTP2,
RP FUNCTION, SUBUNIT, AND INTERACTION WITH LTP2.
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB
RC 10081 / Henssen B9;
RX PubMed=31209106; DOI=10.1074/jbc.ra119.008889;
RA Aggett R., Mallette E., Gilbert S.E., Vachon M.A., Schroeter K.L.,
RA Kimber M.S., Seah S.Y.K.;
RT "The steroid side-chain-cleaving aldolase Ltp2-ChsH2DUF35 is a thiolase
RT superfamily member with a radically repurposed active site.";
RL J. Biol. Chem. 294:11934-11943(2019).
CC -!- FUNCTION: Probably involved in bile acid degradation.
CC {ECO:0000305|PubMed:31209106}.
CC -!- SUBUNIT: Heterodimer composed of ChsH1 and ChsH2. Two heterodimers
CC combine to form an heterotetramer (Probable). The complex interacts
CC with Ltp2 via the DUF35 C-terminal region of ChsH2 (PubMed:31209106).
CC {ECO:0000269|PubMed:31209106, ECO:0000305|PubMed:31209106}.
CC -!- SIMILARITY: Belongs to the thioester dehydratase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001738; ACY99020.1; -; Genomic_DNA.
DR RefSeq; WP_012853804.1; NC_013510.1.
DR PDB; 6OK1; X-ray; 1.70 A; B/D=188-319.
DR PDBsum; 6OK1; -.
DR AlphaFoldDB; D1AB77; -.
DR SMR; D1AB77; -.
DR STRING; 471852.Tcur_3482; -.
DR EnsemblBacteria; ACY99020; ACY99020; Tcur_3482.
DR KEGG; tcu:Tcur_3482; -.
DR eggNOG; COG1545; Bacteria.
DR eggNOG; COG2030; Bacteria.
DR HOGENOM; CLU_057272_0_0_11; -.
DR OMA; TMLQAWT; -.
DR OrthoDB; 1756670at2; -.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR002878; DUF35_OB-fold_C.
DR InterPro; IPR022002; DUF35_Znr_N.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF12172; DUF35_N; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01796; OB_aCoA_assoc; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bile acid catabolism; Lipid degradation; Lipid metabolism;
KW Lyase; Reference proteome; Steroid metabolism.
FT CHAIN 1..319
FT /note="Probable enoyl-CoA hydratase alpha subunit"
FT /id="PRO_0000452242"
FT REGION 199..298
FT /note="DUF35"
FT /evidence="ECO:0000305"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6OK1"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6OK1"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6OK1"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:6OK1"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:6OK1"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:6OK1"
SQ SEQUENCE 319 AA; 35740 MW; C466B73CDC10B8F4 CRC64;
MSGEDYEKRL QAWVGRTLGE PRRGQDPVNV PMIRHWVEAM GDTNPVYLDE EAARATGRET
VVAPASMMQA WTMRGYAATV NPEPEAGGME ELTALLAEGG YTSVVATDSE FEFHRELVPG
DHISVQEQVE SISPEKKTAL GEGRFITTLR TYRDQRGEVV ATQRWRLLRF RPKKTEQTEQ
KPKALRPRPA INRDNAFWFE AAKQRRLVIQ RCAACKTLRH PPGPCCPHCG SFDWDTVEAA
GTGQVYSYIV AHHPPHPAFE MPYVVALVEL TEGTRLVTNL VGIAPDKIEI GMPVVLDWLE
ADPELTLPVF RPAVPQEES
