ID PETD_CHLRE Reviewed; 160 AA. AC P23230; B7U1E5; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 27-MAR-2024, entry version 145. DE RecName: Full=Cytochrome b6-f complex subunit 4 {ECO:0000255|HAMAP-Rule:MF_01344}; DE AltName: Full=17 kDa polypeptide {ECO:0000255|HAMAP-Rule:MF_01344}; GN Name=petD {ECO:0000255|HAMAP-Rule:MF_01344}; OS Chlamydomonas reinhardtii (Chlamydomonas smithii). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae; OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=2137; RX PubMed=2017378; DOI=10.1093/nar/19.4.957; RA Yu W., Spreitzer R.J.; RT "Sequences of trnR-ACG and petD that contain a tRNA-like element within the RT chloroplast genome of Chlamydomonas reinhardtii."; RL Nucleic Acids Res. 19:957-957(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=137c / CC-125; RX PubMed=2060646; DOI=10.1016/0014-5793(91)80698-3; RA Bueschlen S., Choquet Y., Kuras R., Wollman F.A.; RT "Nucleotide sequences of the continuous and separated petA, petB and petD RT chloroplast genes in Chlamydomonas reinhardtii."; RL FEBS Lett. 284:257-262(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC-503; RX PubMed=19473533; DOI=10.1186/1471-2148-9-120; RA Smith D.R., Lee R.W.; RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: RT addressing the mutational-hazard hypothesis."; RL BMC Evol. Biol. 9:120-120(2009). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. RC STRAIN=CC-400; RX PubMed=8421681; DOI=10.1073/pnas.90.2.497; RA Sakamoto W., Kindle K.L., Stern D.B.; RT "In vivo analysis of Chlamydomonas chloroplast petD gene expression using RT stable transformation of beta-glucuronidase translational fusions."; RL Proc. Natl. Acad. Sci. U.S.A. 90:497-501(1993). RN [5] RP IDENTIFICATION, AND COMPLETE PLASTID GENOME. RX PubMed=12417694; DOI=10.1105/tpc.006155; RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., RA Stern D.B.; RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a RT sea of repeats."; RL Plant Cell 14:2659-2679(2002). RN [6] RP CHARACTERIZATION. RC STRAIN=WT12; RX PubMed=7493968; DOI=10.1074/jbc.270.49.29342; RA Pierre Y., Breyton C., Kramer D., Popot J.-L.; RT "Purification and characterization of the cytochrome b6 f complex from RT Chlamydomonas reinhardtii."; RL J. Biol. Chem. 270:29342-29349(1995). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-159. RX PubMed=14647374; DOI=10.1038/nature02155; RA Stroebel D., Choquet Y., Popot J.-L., Picot D.; RT "An atypical haem in the cytochrome b(6)f complex."; RL Nature 426:413-418(2003). CC -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates CC electron transfer between photosystem II (PSII) and photosystem I CC (PSI), cyclic electron flow around PSI, and state transitions. CC -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are CC cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and CC the Rieske protein, while the 4 small subunits are petG, petL, petM and CC petN. The complex functions as a dimer. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- CC pass membrane protein. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the cytochrome b family. PetD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01344}. 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; X56700; CAA40030.1; -; Genomic_DNA. DR EMBL; X72919; CAA51424.1; -; Genomic_DNA. DR EMBL; FJ423446; ACJ50092.1; -; Genomic_DNA. DR EMBL; L05506; AAA84153.1; -; Genomic_DNA. DR EMBL; BK000554; DAA00905.1; -; Genomic_DNA. DR PIR; S16918; S16918. DR RefSeq; NP_958359.1; NC_005353.1. DR PDB; 1Q90; X-ray; 3.10 A; D=1-159. DR PDBsum; 1Q90; -. DR AlphaFoldDB; P23230; -. DR SMR; P23230; -. DR IntAct; P23230; 1. DR STRING; 3055.P23230; -. DR PaxDb; 3055-DAA00905; -. DR GeneID; 2717021; -. DR KEGG; cre:ChreCp002; -. DR eggNOG; KOG4663; Eukaryota. DR HOGENOM; CLU_112652_0_0_1; -. DR InParanoid; P23230; -. DR BioCyc; CHLAMY:CHRECP002-MONOMER; -. DR BioCyc; MetaCyc:CHRECP002-MONOMER; -. DR EvolutionaryTrace; P23230; -. DR Proteomes; UP000006906; Chloroplast. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central. DR GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:UniProtKB-UniRule. DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central. DR GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro. DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC. DR CDD; cd00290; cytochrome_b_C; 1. DR Gene3D; 1.10.287.980; plastocyanin oxidoreductase; 1. DR Gene3D; 1.20.5.510; Single helix bin; 1. DR HAMAP; MF_01344; Cytb6_f_subIV; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR036150; Cyt_b/b6_C_sf. DR InterPro; IPR005870; Cyt_b6/f_cplx_suIV. DR InterPro; IPR048260; Cytochrome_b_C_euk/bac. DR NCBIfam; TIGR01156; cytb6_f_IV; 1. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR PIRSF; PIRSF000033; B6f_17K; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR PROSITE; PS51003; CYTB_CTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Electron transport; Membrane; Photosynthesis; KW Plastid; Reference proteome; Thylakoid; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..160 FT /note="Cytochrome b6-f complex subunit 4" FT /id="PRO_0000061852" FT TRANSMEM 36..56 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344" FT TRANSMEM 95..115 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344" FT TRANSMEM 131..151 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01344" FT CONFLICT 67 FT /note="N -> F (in Ref. 2)" FT /evidence="ECO:0000305" FT HELIX 12..20 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 24..26 FT /evidence="ECO:0007829|PDB:1Q90" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 34..38 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 39..57 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 82..90 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 94..108 FT /evidence="ECO:0007829|PDB:1Q90" FT TURN 109..115 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 127..146 FT /evidence="ECO:0007829|PDB:1Q90" FT HELIX 151..154 FT /evidence="ECO:0007829|PDB:1Q90" SQ SEQUENCE 160 AA; 17442 MW; 6B1C77BBB8E857A8 CRC64; MSVTKKPDLS DPVLKAKLAK GMGHNTYGEP AWPNDLLYMF PVVILGTFAC VIGLSVLDPA AMGEPANPFA TPLEILPEWY FYPVFQILRV VPNKLLGVLL MAAVPAGLIT VPFIESINKF QNPYRRPIAT ILFLLGTLVA VWLGIGSTFP IDISLTLGLF //