ID Q7TUM4_PROMM Unreviewed; 714 AA.
AC Q7TUM4;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|RuleBase:RU362087};
DE EC=6.6.1.1 {ECO:0000256|RuleBase:RU362087};
GN Name=chlD {ECO:0000313|EMBL:CAE22062.1};
GN OrderedLocusNames=PMT_1887 {ECO:0000313|EMBL:CAE22062.1};
OS Prochlorococcus marinus (strain MIT 9313).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74547 {ECO:0000313|EMBL:CAE22062.1, ECO:0000313|Proteomes:UP000001423};
RN [1] {ECO:0000313|EMBL:CAE22062.1, ECO:0000313|Proteomes:UP000001423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9313 {ECO:0000313|Proteomes:UP000001423};
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
CC -!- FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion
CC of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|RuleBase:RU362087}.
CC -!- FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium
CC ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC {ECO:0000256|ARBA:ARBA00003398}.
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 ECO:0000256|RuleBase:RU362087};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis. {ECO:0000256|RuleBase:RU362087}.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799, ECO:0000256|RuleBase:RU362087}.
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DR EMBL; BX548175; CAE22062.1; -; Genomic_DNA.
DR RefSeq; WP_011131253.1; NC_005071.1.
DR AlphaFoldDB; Q7TUM4; -.
DR KEGG; pmt:PMT_1887; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR HOGENOM; CLU_016684_6_2_3; -.
DR OrthoDB; 9775079at2; -.
DR UniPathway; UPA00668; -.
DR Proteomes; UP000001423; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR CDD; cd01451; vWA_Magnesium_chelatase; 1.
DR Gene3D; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041702; BchD/ChlD_VWA.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR012804; Cob_chelat_sub_put.
DR InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR NCBIfam; TIGR02031; BchD-ChlD; 1.
DR NCBIfam; TIGR02442; Cob-chelat-sub; 1.
DR PANTHER; PTHR43473; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43473:SF2; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362087};
KW Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171,
KW ECO:0000256|RuleBase:RU362087};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU362087};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362087};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531,
KW ECO:0000256|RuleBase:RU362087};
KW Reference proteome {ECO:0000313|Proteomes:UP000001423}.
FT DOMAIN 518..710
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 367..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 76558 MW; F5068D3B38DFD04C CRC64;
MVASGSAATA NTRSRDRAGQ DMATRAFPLA AITGHGTLKL SLLLAAVDPE LGGVVIAGGR
GTGKSVLARG LHALLPPIDV LDLEALSKDQ QTSQIHRPIG LNLDPKLPEE WDEASQRLIT
KQGATDEENS KEPLPSRVIP APFVQVPIGI TEDRLVGAVD VTASLTSGTP VFQPGLLAEA
HRGVLYLDEL NLLDDGIVNL MLAAVGAGEN RVEREGLSLS HPCRPLLIAT YNPEEGAMRD
HLLDRFAIAL SADQLISNEQ RVEITEAVLA HGQCSVSFAA KWAQETEALA TQLLLARQWL
PDVQISHAQI EYLVNEAIRG GVEGHRSELY AVRVARAHAA LSGRDQVEAD DLQVAVRLVI
APRALQLPPQ EEQMEPPPPE QQQAPPPPDQ SQEDTSEEDE DEEDDEDTPE EQTSPPVPEE
FMLDPEAIAI DPDLLLFSAA KSKSGNSGNR SAVLSDSRGR YVRPIIPRGP VRRIAVDATL
RAAAPYQKAR RSRQPDRTVI VEEGDLRAKL LQRKAGSLVI FLVDASGSMA LNRMQGAKGA
VIRLLTEAYE NRDEVSLIPF RGEQAEVLLP PTKSITAAKR RLEVMPCGGG SPLAHGLTQA
ARVGANALSK GDLAQVVVVA ITDGRGNVPL GTSLGQPQLE GEDPPDLKQE LLDVASRYRS
LGIKLLVIDT ERKFIGSGMG KDLAEAAAGK YVQLPKATDQ AIAAIAMEAI DQVK
//
