ID FER_SYNY3 STANDARD; PRT; 96 AA. AC P27320; DT 01-AUG-1992 (REL. 23, CREATED) DT 01-AUG-1992 (REL. 23, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE FERREDOXIN. OS SYNECHOCYSTIS SP. (STRAIN PCC 6803). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE. RX MEDLINE; 92338182. RA BOTTIN H., LAGOUTTE B.; RL BIOCHIM. BIOPHYS. ACTA 1101:48-56(1992). RN [2] RP STRUCTURE BY NMR. RX MEDLINE; 96062510. RA LELONG C., SETIF P., BOTTIN H., ANDRE F., NEUMANN J.-M.; RL BIOCHEMISTRY 34:14462-14473(1995). CC -!- FUNCTION: FERREDOXIN ARE IRON-SULFUR PROTEINS THAT TRANSFER CC ELECTRONS IN A WIDE VARIETY OF METABOLIC REACTIONS. CC -!- THE MIDPOINT REDOX POTENTIAL FOR THIS PROTEIN IS -412 MV. CC -!- COFACTOR: BINDS A 2FE-2S CLUSTER. 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 PDB; 1DOX; PRELIMINARY. DR PROSITE; PS00197; 2FE2S_FERREDOXIN. KW ELECTRON TRANSPORT; IRON-SULFUR; 3D-STRUCTURE. FT METAL 39 39 IRON-SULFUR (2FE-2S). FT METAL 44 44 IRON-SULFUR (2FE-2S). FT METAL 47 47 IRON-SULFUR (2FE-2S). FT METAL 77 77 IRON-SULFUR (2FE-2S). FT DISULFID 18 85 PROBABLE. SQ SEQUENCE 96 AA; 10232 MW; 04C0ED7E CRC32; ASYTVKLITP DGESSIECSD DTYILDAAEE AGLDLPYSCR AGACSTCAGK ITAGSVDQSD QSFLDDDQIE AGYVLTCVAY PTSDCTIETH KEEDLY //