ID Q01B26_OSTTA Unreviewed; 1397 AA.
AC Q01B26; A0A1Y5IIK9; A0A454XJ91;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN ORFNames=BE221DRAFT_188678 {ECO:0000313|EMBL:OUS49406.1},
GN OT_ostta04g02090 {ECO:0000313|EMBL:CAL51621.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CAL51621.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
RN [2] {ECO:0000313|EMBL:CAL51621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCC4221 {ECO:0000313|EMBL:CAL51621.1};
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S., Ral J.P., Bouget F.Y.,
RA Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 131:11647-11652(2006).
RN [3] {ECO:0000313|EMBL:CAL51621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCC4221 {ECO:0000313|EMBL:CAL51621.1};
RX PubMed=25494611; DOI=10.1186/1471-2164-15-1103;
RA Blanc-Mathieu R., Verhelst B., Derelle E., Rombauts S., Bouget F.Y.,
RA Carre I., Chateau A., Eyre-Walker A., Grimsley N., Moreau H., Piegu B.,
RA Rivals E., Schackwitz W., Van de Peer Y., Piganeau G.;
RT "An improved genome of the model marine alga Ostreococcus tauri unfolds by
RT assessing Illumina de novo assemblies.";
RL BMC Genomics 15:1103-1103(2014).
RN [4] {ECO:0000313|EMBL:OUS49406.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC 1115 {ECO:0000313|EMBL:OUS49406.1};
RG DOE Joint Genome Institute;
RA Blanc-Mathieu R., Krasovec M., Hebrard M., Yau S., Desgranges E.,
RA Martin J., Schackwitz W., Kuo A., Salin G., Donnadieu C., Desdevises Y.,
RA Sanchez-Ferandin S., Moreau H., Rivals E., Grigoriev I.V., Grimsley N.,
RA Eyre-Walker A., Piganeau G.;
RT "Population genomics of picophytoplankton unveils novel chromosome
RT hypervariability.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-
CC protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306,
CC ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001499};
CC -!- PATHWAY: Porphyrin-containing compound metabolism.
CC {ECO:0000256|ARBA:ARBA00023444}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family.
CC {ECO:0000256|ARBA:ARBA00010851}.
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DR EMBL; CAID01000004; CAL51621.1; -; Genomic_DNA.
DR EMBL; KZ155771; OUS49406.1; -; Genomic_DNA.
DR RefSeq; XP_003078741.1; XM_003078693.1.
DR STRING; 70448.Q01B26; -.
DR GeneID; 9834059; -.
DR KEGG; ota:OT_ostta04g02090; -.
DR InParanoid; Q01B26; -.
DR OMA; WETGQAM; -.
DR OrthoDB; 1199959at2759; -.
DR Proteomes; UP000009170; Chromosome 4.
DR Proteomes; UP000195557; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR CDD; cd10150; CobN_like; 1.
DR InterPro; IPR011771; BchH.
DR InterPro; IPR003672; CobN/Mg_chltase.
DR InterPro; IPR022571; Mg_chelatase_H_N.
DR NCBIfam; TIGR02025; BchH; 1.
DR PANTHER; PTHR44119; MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC; 1.
DR PANTHER; PTHR44119:SF1; MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC; 1.
DR Pfam; PF02514; CobN-Mg_chel; 1.
DR Pfam; PF11965; DUF3479; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT DOMAIN 89..249
FT /note="Magnesium chelatase subunit H N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11965"
FT REGION 17..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1369..1396
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 47..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1397 AA; 153712 MW; 9040CA35BA37AE7A CRC64;
MSGTTRALAF RGVGSTTAFK GKNGAKPARR VAPTTRAVAT GPKGPLKKKG SNEEDKIEDM
SSGSRGMFTT VDPEVRRIVP DAKGRVVVKV TYVVLESQYQ SALSAAVKQI NETNDKVCVE
VVGYLLEELR NKDNLEALKK DVETSNIFIG SLIFIEELAE KIVEIVQPCR EKLDACLIFP
SMPQVMRLNK LGTFSMAQLG QSKSAIASFM RKKKESGGFE EGMLKLVRTL PKVLKYLPSD
KAADARNFMN SLQYWLGGST DNLENFLLMI SKAYVPELKG VDLTVAEPEV FPDVGIWHPS
APVYYEDLKE YLNWYDTRKD IKFKADSPVI GLVLQRSHLV TGDHGHYDGM VMELEAKGAR
VVPIFAGGLD FSGPIEKFFF DPITKGAYVD TVLSLTGFAL VGGPARQDHP KAIESLKKLN
VPYMVTVPLS FQTTEEWKDS TLGLHPVQVA LQVALPELDG GLEPMIFSGR DSKSGKSHTL
EDRAAQIANR AIKWAALRKK TAAAKKLAIT VFSFPPDKGN VGTAAYLNVF GSIYRVLQGL
RRQGYNVGVL PSSEEELINS VLNDKEAQYA SPDMNVAYRM PVNEYKKLCI YEEDLHENWG
PPPGNLNTDG QNMLVYGKQF GNVFIGVQPT FGYEGDPMRL LFSKSASPHH GFAAYYTYLE
HIFQADAVLH FGTHGSLEFM PGKQVGMAGV CYPDRLIGNI PNIYYYAANN PSEATIAKRR
SYANTISYLT PPAENAGLYK GLKELKELIS SYQTLKDSGR GPSIVNTIIS TAITCNLDKD
VKEIPTDPEA DAADFDSDRR DLIVGKVYQK LMEIESRLLP CGLHVVGCPP SAEEAVATLV
NIASIDREDE GIIALPGLLA MSIGRDIESI YRSNDAGNLE DVQLLQDITE ACRACVRTFV
SSAADPSGRV AAGALASVGK LFGSAAVALP WGDALKGTQF ESTDVEKMRT LFDYLRFCLE
QVVKDNELGA LTEALEGQYV LPGPGGDPIR NPKVLPTGKN IHALDPQAIP TGAAVASAKV
VVDRLIEREK NENGGKYPES IALVLWGTDN IKTYGESLAQ VMLMVGVRPA PDALGRVNKL
ELISLEELGR PRIDVVVNCS GVFRDLFVNQ MNLLDRAVKL AAEQENEPDE MNFVRKHAKE
QAAELGLSVR EAATRIFSNA SGSYSSNVNL AVENSSWNDE SQLQDMYLNR KSFAFNSDAP
GAGMETKKEL FESALSKVDV TFQNLDSSEI SLTDVSHYFD SDPTKLVQGV RKDGKMPSSY
IADTTTANAQ VRSLSETMRL DSRTKLLNPK WYEGMMASGY EGTREIQKRL NNTLGWSATS
GQVDNWVYED ANSTFMADPE MQKRLMESNP NSFRKMVANF LEANGRGYWE TSEENIERLK
QLYMEVEDRI EGVENGA
//
