ID   PORB_HORVU              Reviewed;         395 AA.
AC   Q42850;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 122.
DE   RecName: Full=Protochlorophyllide reductase B, chloroplastic;
DE            Short=PCR B;
DE            EC=1.3.1.33;
DE   AltName: Full=NADPH-protochlorophyllide oxidoreductase B;
DE            Short=POR B;
DE   Flags: Precursor;
GN   Name=PORB;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7724548; DOI=10.1073/pnas.92.8.3254;
RA   Holtorf H., Reinbothe S., Reinbothe C., Bereza B., Apel K.;
RT   "Two routes of chlorophyllide synthesis that are differentially regulated
RT   by light in barley (Hordeum vulgare L.).";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3254-3258(1995).
CC   -!- FUNCTION: Phototransformation of protochlorophyllide (Pchlide) to
CC       chlorophyllide (Chlide).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chlorophyllide a + NADP(+) = H(+) + NADPH +
CC         protochlorophyllide a; Xref=Rhea:RHEA:11132, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:83348,
CC         ChEBI:CHEBI:83350; EC=1.3.1.33;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- INTERACTION:
CC       Q42850; P13653: PORA; NbExp=2; IntAct=EBI-15724755, EBI-15724741;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. POR subfamily. {ECO:0000305}.
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DR   EMBL; X84738; CAA59228.1; -; mRNA.
DR   PIR; S52285; S52285.
DR   AlphaFoldDB; Q42850; -.
DR   SMR; Q42850; -.
DR   DIP; DIP-46279N; -.
DR   IntAct; Q42850; 1.
DR   EnsemblPlants; HORVU.MOREX.r2.1HG0036700.1; HORVU.MOREX.r2.1HG0036700.1; HORVU.MOREX.r2.1HG0036700.
DR   EnsemblPlants; HORVU.MOREX.r2.1HG0036700.1.mrna1; HORVU.MOREX.r2.1HG0036700.1.mrna1; HORVU.MOREX.r2.1HG0036700.1.
DR   Gramene; HORVU.MOREX.r2.1HG0036700.1; HORVU.MOREX.r2.1HG0036700.1; HORVU.MOREX.r2.1HG0036700.
DR   Gramene; HORVU.MOREX.r2.1HG0036700.1.mrna1; HORVU.MOREX.r2.1HG0036700.1.mrna1; HORVU.MOREX.r2.1HG0036700.1.
DR   BRENDA; 1.3.1.33; 2687.
DR   UniPathway; UPA00668; -.
DR   ExpressionAtlas; Q42850; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016630; F:protochlorophyllide reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd09810; LPOR_like_SDR_c_like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005979; Prochl_reduct.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01289; LPOR; 1.
DR   PANTHER; PTHR44419; PROTOCHLOROPHYLLIDE REDUCTASE C, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR44419:SF15; PROTOCHLOROPHYLLIDE REDUCTASE C, CHLOROPLASTIC; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   1: Evidence at protein level;
KW   Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase;
KW   Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..395
FT                   /note="Protochlorophyllide reductase B, chloroplastic"
FT                   /id="PRO_0000023294"
SQ   SEQUENCE   395 AA;  42148 MW;  BFCB90122D6F64B9 CRC64;
     MALQAATSFL PSALSARKEG AAKDSAFFGV RLADGLKLDA TSLGLRTKRV NTSSVAIRAQ
     AAAVSAPTAT PASPAGKKTV RTGNAIITGA SSGLGLATAK ALAESGKWHV IMACRDYLKT
     ARAARAAGMP KGSYTIVHLD LASLDSVRQF VKNVRQLDMP IDVVVCNAAV YQPTAKEPSF
     TADGFEMSVG VNHLGHFLLA RELLEDLKAS DYPSKRLIIV GSITGNTNTL AGNVPPKANL
     GDLRGLAAGL NGVGSAAMID GAEFDGAKAY KDSKVCNMLT MQEFHRRYHE ETGVTFASLY
     PGCIATTGLF REHIPLFRLL FPPFQKYITK GYVSEEEAGK RLAQVVSEPS LTKSGVYWSW
     NKNSASFENQ LSEEASDTEK ARKVWELSEK LVGLA
//