| Tag | Content |
|---|
| CPLM ID | CPLM-015045 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Light-independent protochlorophyllide reductase subunit N |
Protein Synonyms/Alias | DPOR subunit N; LI-POR subunit N |
Gene Name | bchN |
Gene Synonyms/Alias | RPA1542 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 297 | ERALSAFKSELGGRR | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent (By similarity). |
Sequence Annotation | |
Keyword | Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Complete proteome; Oxidoreductase; Photosynthesis. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 429 AA |
Protein Sequence | MTVHVTGCST ATADQLVSRE IRTESGQREV FCGLTGIVWL HRKIQDAFFL VVGSRTCAHL 60
VQSAAGVMIF AEPRFGTAIM EEKDLAGLTD ANDELDRVVT QLLARRPDIK LLFLVGSCPS 120
EVIKLDLSRA ALRLSQRFSP GVRILNYSGS GIETTFTQGE DACLASLVPE LPAQTDTKPS 180
LLVVGSLADV VEDQFARMFE ALGVGNVAFF PPRKSTALPS VGPNTKILMA QPFLPDTVRA 240
LEERGAKRLA APFPLGVEGT TGWLRAAADA FGVDPAKFEQ VTAPNRARAE RALSAFKSEL 300
GGRRIFFFPD SQLEIPLARF LSRELDMQLV EVATPYLHRE HLAEELKLLP IEVALTEGQD 360
VDDQLDRCRI ARPDIVVCGL GLANPLEAEG ITTKWSIELV FTPIQGYEQA ADLAELFARP 420
LVRRAKLVA 429 |
Gene Ontology | GO:0016730; F:oxidoreductase activity, acting on iron-sulfur proteins as donors; IEA:HAMAP. GO:0036070; P:light-independent bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway. GO:0019685; P:photosynthesis, dark reaction; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |