ID A0A0G4KC33_9FLOR Unreviewed; 751 AA. AC A0A0G4KC33; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 05-DEC-2018, entry version 12. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000256|HAMAP-Rule:MF_00458}; DE EC=1.97.1.12 {ECO:0000256|HAMAP-Rule:MF_00458}; DE AltName: Full=PsaA {ECO:0000256|HAMAP-Rule:MF_00458}; GN Name=psaA {ECO:0000256|HAMAP-Rule:MF_00458, GN ECO:0000313|EMBL:CRF40148.1}; OS Laurencia snackeyi. OG Plastid {ECO:0000313|EMBL:CRF40148.1}. OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; OC Ceramiales; Rhodomelaceae; Laurencieae; Laurencia. OX NCBI_TaxID=1858662 {ECO:0000313|EMBL:CRF40148.1}; RN [1] {ECO:0000313|EMBL:CRF40148.1} RP NUCLEOTIDE SEQUENCE. RA Verbruggen Heroen; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced CC [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]- CC [ferredoxin]; Xref=Rhea:RHEA:30407, ChEBI:CHEBI:29036, CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:49552, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040; EC=1.97.1.12; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00458}; CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00458}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000256|HAMAP- CC Rule:MF_00458}. 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; LN833431; CRF40148.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule. DR GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR Gene3D; 1.20.1130.10; -; 1. DR HAMAP; MF_00458; PSI_PsaA; 1. DR InterPro; IPR006243; PSI_PsaA. DR InterPro; IPR001280; PSI_PsaA/B. DR InterPro; IPR020586; PSI_PsaA/B_CS. DR InterPro; IPR036408; PSI_PsaA/B_sf. DR PANTHER; PTHR30128:SF8; PTHR30128:SF8; 1. DR Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; SSF81558; 1. DR TIGRFAMs; TIGR01335; psaA; 1. DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00458}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_00458}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_00458}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00458}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00458}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00458}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00458}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00458, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00458}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00458}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00458}; KW Photosystem I {ECO:0000256|HAMAP-Rule:MF_00458}; KW Plastid {ECO:0000313|EMBL:CRF40148.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00458}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00458}. FT TRANSMEM 73 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 353 373 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 393 415 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 436 457 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 538 557 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 592 612 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 665 687 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 728 748 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 575 575 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT METAL 584 584 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT METAL 676 676 Magnesium (chlorophyll-a' A1 axial FT ligand; P700 special pair). FT {ECO:0000256|HAMAP-Rule:MF_00458}. FT METAL 684 684 Magnesium (chlorophyll-a A3 axial FT ligand). {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT BINDING 692 692 Chlorophyll-a A3. {ECO:0000256|HAMAP- FT Rule:MF_00458}. FT BINDING 693 693 Phylloquinone A. {ECO:0000256|HAMAP-Rule: FT MF_00458}. SQ SEQUENCE 751 AA; 83790 MW; 685A1C8CA89390E8 CRC64; MTTSSKEQET NKVKVSVDKN PVTTSFEKWA KPGHFSRTLA KGPNTTTWIW NLHADAHDFD SHTNSLEDIS RKIFSAHFGQ LAIIFLWLSG MYFHGARFSN YVAWLNNPTL IKPSAQVVWP IVGQEILNAD VGGGFQGVQI TSGFFQLWRS SGITTEFELY ATAIGGLFMS LLMVFAGWFH YHKSAPKLEW FQNVESMMNH HLAGLLGLGC LGWSGHQIHI ALPINKLLDS GVSPQEIPLP HEFIVNRSLM SELYPSFSKG ILPFFTLNWS EYSDFLTFKG GLNPINGGLW LSDIAHHHLA LSVMFLVAGH MYRTNWGIGH SMKEILEAHK GPFTGEGHKG LYEILTTSWH AQLAINLAMM GSLSIIVAHH MYAMPPYPYI ATDYATQLSL FTHHMWIGGF CVVGAGAHAS IFMVRDYNPA QNYDNVLDRV IRHRDAIISH LNWLCIFLGF HSFGLYIHND TMRALGRSQD MFSDTGIQLQ PIFAQWIQNI HTLAPSNTSP NSLATASYAF GGDTIAVANK IAMMPIKLGT ADFMVHHIHA FTIHVTVLIL VKGFLFARNS RLIPDKSNLG FRFPCDGPGR GGTCQVSAWD HVFLGLFWMY NSLSIVIFHF SWKMQSDVWG SIKGTEISHI AGGNFSQSAI TINGWLRDFL WAQASQVIQS YGSALSAYGL IFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKVKVA PSIQPRALSI TQGRAVGLAH YLLGGIGTTW AFFLARIISL G //