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Database: UniProt
Entry: M2XEW1_GALSU
LinkDB: M2XEW1_GALSU
Original site: M2XEW1_GALSU 
ID   M2XEW1_GALSU            Unreviewed;       549 AA.
AC   M2XEW1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   18-JUN-2025, entry version 43.
DE   RecName: Full=Cytochrome c-553 {ECO:0000256|ARBA:ARBA00033211};
DE   AltName: Full=Cytochrome c553 {ECO:0000256|ARBA:ARBA00031247};
DE   AltName: Full=Soluble cytochrome f {ECO:0000256|ARBA:ARBA00030448};
GN   ORFNames=Gasu_40720 {ECO:0000313|EMBL:EME28527.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME28527.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
CC   -!- FUNCTION: Functions as an electron carrier between membrane-bound
CC       cytochrome b6-f and photosystem I in oxygenic photosynthesis.
CC       {ECO:0000256|ARBA:ARBA00002347}.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of biotin
CC       carboxyl carrier protein, biotin carboxylase and 2 subunits each of
CC       ACCase subunit alpha and ACCase plastid-coded subunit beta (accD).
CC       {ECO:0000256|ARBA:ARBA00011842}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC       {ECO:0000256|ARBA:ARBA00004456}.
CC   -!- SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.
CC       {ECO:0000256|ARBA:ARBA00009650}.
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DR   EMBL; KB454519; EME28527.1; -; Genomic_DNA.
DR   RefSeq; XP_005705047.1; XM_005704990.1.
DR   AlphaFoldDB; M2XEW1; -.
DR   STRING; 130081.M2XEW1; -.
DR   EnsemblPlants; EME28527; EME28527; Gasu_40720.
DR   GeneID; 17087360; -.
DR   Gramene; EME28527; EME28527; Gasu_40720.
DR   KEGG; gsl:Gasu_40720; -.
DR   eggNOG; KOG0540; Eukaryota.
DR   OrthoDB; 10053020at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:InterPro.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:TreeGrafter.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   FunFam; 1.10.760.10:FF:000038; Cytochrome c6; 1.
DR   Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 1.
DR   Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR   HAMAP; MF_01395; AcetylCoA_CT_beta; 1.
DR   HAMAP; MF_00594; Cytc_PetJ; 1.
DR   HAMAP; MF_01378; PSII_Cyt550; 1.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR000438; Acetyl_CoA_COase_Trfase_b_su.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR023655; Cyt_C6.
DR   InterPro; IPR029490; Cytochrom_C550.
DR   InterPro; IPR017851; PsbV_cyt_c550.
DR   NCBIfam; TIGR00515; accD; 1.
DR   NCBIfam; NF045930; Cytc6PetJCyano; 1.
DR   NCBIfam; TIGR03045; PS_II_C550; 1.
DR   PANTHER; PTHR42995; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR42995:SF5; ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT BETA, CHLOROPLASTIC; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF14495; Cytochrom_C550; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   PRINTS; PR01070; ACCCTRFRASEB.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 2.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS51007; CYTC; 2.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Ligase {ECO:0000313|EMBL:EME28527.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Photosystem II {ECO:0000256|ARBA:ARBA00023276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EME28527.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          51..320
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          350..449
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          463..543
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
SQ   SEQUENCE   549 AA;  60811 MW;  1AB36AA30CF285DF CRC64;
     MSNGLDNINN DNIIKDFQRV IRNKIKLNSI RTTKRLHNLK QIKPLQIRQG IWFICPCCEN
     TLPRAQLEKK SYICIYCNYY FPLPSHKRIQ EIIDQNTWTP INTNLISTDP LGFYDIKAYN
     SRLEENKIKT KLQDAVETGI GLINGIKVAC AVMDFRFMGG SMGSAVGEKI TRLIEQATLY
     KLPVIIFCAS GGARMQEGIL SLMQMAKISS VLAKHKNASL LYISVLTSPT TGGVTASFGM
     LGDIIIAEPR AVVAFAGRRV IEQTIKQKLP PDFQIAELLW KKGFVDLIIQ RTELKNKLYQ
     LLRLHCQIAI LSIIYIIISN ANLASANDLD EKSRTVLLNE NGKTITLTTE QVKKGKRLFN
     SNCAQCHSGG GTKTNPNIGL DIKSLQSATP KRDNIEALID YMKNPTTYDG TESIAEIHPS
     IKSADIFPKM RNMTDDDLFA IAGHILLQSN IASEKWGGVA FAADLSNGEQ IFSANCAACH
     TGGNNVIMPE KTLKKESLEA NKVNTVEAIT YQVTNGKNAM PAFGGRLSDT DIEDVANYIL
     TQAEKGWSN
//
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