ID   TC32B_BRANA             Reviewed;         320 AA.
AC   A0A078ISJ6;
DT   13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Short-chain dehydrogenase TIC 32 B, chloroplastic {ECO:0000305};
DE            EC=1.1.1.- {ECO:0000305};
DE   AltName: Full=Translocon at the inner envelope membrane of chloroplasts 32 B {ECO:0000305};
DE            Short=BnTIC32B {ECO:0000305};
GN   Name=TIC32B {ECO:0000305};
GN   Synonyms=BnaC04g53630D {ECO:0000312|EMBL:CDY52816.1};
GN   ORFNames=GSBRNA2T00007890001 {ECO:0000312|EMBL:CDY52816.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh;
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
CC   -!- FUNCTION: Involved in protein precursor import into chloroplasts.
CC       {ECO:0000250|UniProtKB:A2RVM0}.
CC   -!- SUBUNIT: Part of the Tic complex. {ECO:0000250|UniProtKB:A2RVM0}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC       {ECO:0000250|UniProtKB:A2RVM0}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; LK033133; CDY52816.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078ISJ6; -.
DR   SMR; A0A078ISJ6; -.
DR   EnsemblPlants; CDY52816; CDY52816; GSBRNA2T00007890001.
DR   Gramene; CDY52816; CDY52816; GSBRNA2T00007890001.
DR   OMA; CINTHKD; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Calmodulin-binding; Chloroplast; Membrane; NADP; Oxidoreductase; Plastid;
KW   Plastid inner membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..320
FT                   /note="Short-chain dehydrogenase TIC 32 B, chloroplastic"
FT                   /id="PRO_0000448490"
FT   REGION          301..317
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RVV4"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00334"
FT   BINDING         40..46
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         92..93
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         119
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         140
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KES3"
SQ   SEQUENCE   320 AA;  34865 MW;  3A65B2CFEF28434E CRC64;
     MEIYGMVTGK AGKSGYGSAS TAEDVTHSID AKHLTAIITG GTSGIGLEAA RVLGMRGAHV
     IIAARNTKAA NDSKEMILQM YPNARIDCLQ LDLSSIKSVR SFIHQFLALN VPLNILINNA
     GVMFCPFQLS EDGIESQFAT NHIGHFLLTN LLLDKMKSSA RESGIEGRIV NLSSIAHTYT
     YTEGIMFDYI NDPDRYSEKK AYGQSKLANL LHSNALSRKL QEEGVNITIN SVHPGLITTN
     LFRHSGLGMA VLKAMSFFLW KNIPQGAATT CYVALHPDLK GVTGKYFTDC NVTTPSNFAI
     DTTLADKLWD FSIKLVDSLP