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Database: UniProt
Entry: K0RAM2_THAOC
LinkDB: K0RAM2_THAOC
Original site: K0RAM2_THAOC 
ID   K0RAM2_THAOC            Unreviewed;      1459 AA.
AC   K0RAM2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=magnesium chelatase {ECO:0000256|ARBA:ARBA00012825};
DE            EC=6.6.1.1 {ECO:0000256|ARBA:ARBA00012825};
GN   ORFNames=THAOC_35247 {ECO:0000313|EMBL:EJK46106.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK46106.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK46106.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK46106.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJK46106.1}.
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DR   EMBL; AGNL01047989; EJK46106.1; -; Genomic_DNA.
DR   EnsemblProtists; EJK46106; EJK46106; THAOC_35247.
DR   eggNOG; ENOG502RFFJ; Eukaryota.
DR   OMA; GYWNAGG; -.
DR   Proteomes; UP000266841; 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266841};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1459
FT                   /note="magnesium chelatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003836173"
FT   DOMAIN          106..271
FT                   /note="Magnesium chelatase subunit H N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11965"
FT   REGION          65..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1459 AA;  157260 MW;  245B8BA1668C1FAA CRC64;
     MHSAIGTPPL AAALLLILQL LSGPSPLRAF APAGGVLLRT RPSIVRGRSP SRRGGVRVPA
     RTVFEVERSP TREDEASSAP PPIAEGRGGA GDVDSDEGNT TRATNVVLLA GFESFNRELY
     EQSGRLLPPS LGPVSVKVFA DSDIRGNASG EFATAVGEAD VFLASLVFDY DDVSAVTAML
     DSAEDGRTQK TRLIFECATE LMEYNRVGSF SMASAGDGPS GPPPAVKAVL SKFSSGREED
     KLAGYLELLK VGPELLKFVP GEKAGDLRTW MEAYRYWNQG GLSNVRSMLQ LLVSKMRKNA
     AAAANAGDLT LPELVVTPAT GLLHPLLVDE SGSMAYASDP KSYMDWRLSS ACAKSAKERK
     FPLAPDDAPR VALLLYRKHV ITGQRYIADL IRAMEAEGLM PVPVFINGVE AHAIVRDWLT
     SDREVEKVNS GAATREPTYK PNEAAEVDAV VNTIGFPLVG GPAGSMEAGR NVDLSSKLLS
     DMDVPYVVAS PLLLQSITTW KECGVLGLQS VVLYSLPELD GAVDTVVLGG LVGDKIALVP
     ERVRKLAGRL NGWVGLRRTP VKDRRISVVL YGFPPNVGAV GTAALLDVPS SLDNLLKRLD
     KEGYNVGKYA SDPNSSGESL VAALSVLCEN AVIAGGFERM QSAVEVRMER ARGGDPTVAE
     TLARPGGGLG GAVVKGANVE FDDLENMLGK YMARKVRRAW PESERGPGVN AKNEMVVSGL
     QLGNVFVTVQ PLLGVEGDPM RLLFERDLTP HPQYCAAYKY MQSGEDEGGA GSQAVVHLGM
     HGTVEWLPGQ PLGNDRQSWS DELLGSLPNV YVYAANNPSE SILAKRRGYG TLVSYNVPPY
     GRAGLYLELA SLKDLVNEFR SDSAESRADL RESILAQCER TGLTSDISPP CDDADEESFD
     DYITSLSNYL VELEERLFSS GLHTLGDAPT DLELASYLNA YFAGRLNDAE VEDVVRQSRV
     KRERTDENAF NVLAFLAWLA DLAGGGARED AVGDVSDEKA SLMQEGLEVA DLLKKNAEEL
     NSVMTALDGG YVKPAPGGDL LRDGTSVLPT GRNIHALDPY RMPSAGASAR GTRAADEIIR
     QHLEANGGVY PETVAVTLWG LDTIKTRGEA IAIVLALVGA RAVREGTGRT VCFELIPLEE
     LGRPRIDILA SLSGIFRDSF ANVVDLLDDM FERAATADES PNMNFIRKHA AELEAAGTER
     PAARLFSNPP GDYGSMVNEV VGTGDWEDEA SLGEVWKSRN AYSYGRSEGG GGTKSGTSRP
     EVLNKLLATT ERIVQEIDSV EYGLTDIQEY YSNTGALKKA AENRKPIDKS TGKAQKVAVS
     VIEAFGGPRT DDDCVPVRDV EEVLRIEYRS KLLNPKWRDA MLEQGSGGAY EVSQRMTAMI
     GWAATAEVDN FVFDQAAERY ALDEEVAAKL QKNNPEAFKN VVRRLLEASG RGMWETDDET
     IEKLKSLYAD ADDLVEQVR
//
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