ID POR_SYNY3 Reviewed; 322 AA. AC Q59987; Q55825; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 145. DE RecName: Full=Light-dependent protochlorophyllide reductase; DE Short=PCR; DE EC=1.3.1.33; DE AltName: Full=NADPH-protochlorophyllide oxidoreductase; DE Short=LPOR; DE Short=POR; GN Name=por; Synonyms=pcr; OrderedLocusNames=slr0506; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7731978; DOI=10.1073/pnas.92.9.3749; RA Suzuki J.Y., Bauer C.E.; RT "A prokaryotic origin for light-dependent chlorophyll biosynthesis of RT plants."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3749-3753(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). 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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. POR subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA68281.1; Type=Erroneous initiation; Evidence={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; L37783; AAA68281.1; ALT_INIT; Genomic_DNA. DR EMBL; BA000022; BAA10580.1; -; Genomic_DNA. DR PIR; S76636; S76636. DR PDB; 6L1G; X-ray; 2.20 A; A/B=1-322. DR PDB; 6R48; X-ray; 1.87 A; A/B=5-322. DR PDBsum; 6L1G; -. DR PDBsum; 6R48; -. DR AlphaFoldDB; Q59987; -. DR SMR; Q59987; -. DR IntAct; Q59987; 4. DR STRING; 1148.gene:10500084; -. DR PaxDb; 1148-1001743; -. DR EnsemblBacteria; BAA10580; BAA10580; BAA10580. DR KEGG; syn:slr0506; -. DR eggNOG; COG1028; Bacteria. DR InParanoid; Q59987; -. DR PhylomeDB; Q59987; -. DR BRENDA; 1.3.1.33; 382. DR UniPathway; UPA00668; -. DR Proteomes; UP000001425; Chromosome. 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 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 3D-structure; Chlorophyll biosynthesis; NADP; Oxidoreductase; KW Photosynthesis; Reference proteome. FT CHAIN 1..322 FT /note="Light-dependent protochlorophyllide reductase" FT /id="PRO_0000219917" FT CONFLICT 23 FT /note="A -> R (in Ref. 1; AAA68281)" FT /evidence="ECO:0000305" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:6R48" FT TURN 13..15 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 17..28 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 40..49 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 67..79 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 110..115 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 117..132 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 150..153 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 169..172 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 189..215 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 231..243 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:6L1G" FT HELIX 258..270 FT /evidence="ECO:0007829|PDB:6R48" FT HELIX 272..274 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:6R48" FT STRAND 295..298 FT /evidence="ECO:0007829|PDB:6L1G" FT HELIX 304..318 FT /evidence="ECO:0007829|PDB:6R48" SQ SEQUENCE 322 AA; 36062 MW; B805C95E139EA213 CRC64; MEQPMKPTVI ITGASSGVGL YGAKALIDKG WHVIMACRNL DKTQKVADEL GFPKDSYTII KLDLGYLDSV RRFVAQFREL GRPLKALVCN AAVYFPLLDE PLWSADDYEL SVATNHLGHF LLCNLLLEDL KACPDADKRL IILGTVTANS KELGGKIPIP APPDLGNFEG FEAGFKKPIA MINNKKFKSG KAYKDSKLCN MLTTRELHRR FHQETGIVFN SLYPGCVADT PLFRNHYSLF RTIFPWFQKN VTKGYVSQEL AGERVAMVVA DDKFKDSGVH WSWGNRQQAG REAFVQELSE QGSDAQKAQR MWDLSEKLVG LV //