BCHD_CERS4
ID BCHD_CERS4 Reviewed; 558 AA.
AC O34845; Q3J187;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Magnesium-chelatase 60 kDa subunit;
DE Short=Mg-chelatase subunit D;
DE EC=6.6.1.1;
DE AltName: Full=Mg-protoporphyrin IX chelatase;
GN Name=bchD; OrderedLocusNames=RHOS4_18790; ORFNames=RSP_0274;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hansson M., Kannangara C.G.;
RT "Rhodobacter sphaeroides bchI and bchD encoding two subunits of magnesium
RT chelatase.";
RL (er) Plant Gene Register PGR97-190(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10648776; DOI=10.1093/nar/28.4.862;
RA Choudhary M., Kaplan S.;
RT "DNA sequence analysis of the photosynthesis region of Rhodobacter
RT sphaeroides 2.4.1.";
RL Nucleic Acids Res. 28:862-867(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION.
RX PubMed=7892204; DOI=10.1073/pnas.92.6.1941;
RA Gibson L.C.D., Willows R.D., Kannangara C.G., von Wettstein D.,
RA Hunter C.N.;
RT "Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides:
RT reconstitution of activity by combining the products of the bchH, -I, and
RT -D genes expressed in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1941-1944(1995).
CC -!- FUNCTION: Involved in bacteriochlorophyll biosynthesis; introduces a
CC magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
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 -!- PATHWAY: Porphyrin-containing compound metabolism; bacteriochlorophyll
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000305}.
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DR EMBL; AJ010302; CAB38736.1; -; Genomic_DNA.
DR EMBL; AF017642; AAB97157.1; -; Genomic_DNA.
DR EMBL; AF195122; AAF24286.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79447.2; -; Genomic_DNA.
DR PIR; T50742; T50742.
DR RefSeq; WP_017140264.1; NZ_CP030271.1.
DR RefSeq; YP_353348.2; NC_007493.2.
DR AlphaFoldDB; O34845; -.
DR SMR; O34845; -.
DR STRING; 272943.RSP_0274; -.
DR PRIDE; O34845; -.
DR EnsemblBacteria; ABA79447; ABA79447; RSP_0274.
DR KEGG; rsp:RSP_0274; -.
DR PATRIC; fig|272943.9.peg.2217; -.
DR eggNOG; COG1240; Bacteria.
DR OMA; DTQMNYL; -.
DR BioCyc; MetaCyc:MON-13262; -.
DR UniPathway; UPA00669; -.
DR Proteomes; UP000002703; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR011776; Mg_chelatase_ATPase-dsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR02031; BchD-ChlD; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Ligase; Nucleotide-binding; Photosynthesis; Reference proteome.
FT CHAIN 1..558
FT /note="Magnesium-chelatase 60 kDa subunit"
FT /id="PRO_0000206853"
FT DOMAIN 376..555
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 234..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 58548 MW; 2A16F62C1268FB3A CRC64;
MPLGPWERVE AALTLLAIDP AGLKGLWLRA RASALRDRIT GALGALPLPV RRIHPTIGDD
ALFGGLDLAA TLSAGTPVVQ KGILDEPAVL VLAMAERTLP GLAARLGTAL DAPRHCLIAL
DEGAERDELL PLGLVDRLAL FLDLDGLPWG ETREIALDPE RLAAARARLA AVATPPEAAA
TLARVAAQLG IASLRAPTLA LAAARAQAAW EGHAAVTDED IRRAADLVFA HRAMPASEEA
PPEPEPEPPE DQPDDSPPPP EQQQGEEMFP EEMLVEAVRA ALPADLLEQL AAGRAARMAR
GATGTGSAKA GNRRGRPLPS RMGRLGTGAR IDLVGTLRAA APWQPLRRRQ QKTDAVLLVR
PSDIRIKRFR ETSDRVLIFA VDASGSSAMA RLSEAKGAVE LLLGQAYARR DHVSLLAFRG
RDAELILPPT RSLVQTKRRL AGLPGGGGTP LAHGLRLALA VGLQARARGM TPTVALLTDG
RGNIALDGSA NRAQAEEDAL KLAASLRGSG LPAVVIDTAN RPQPSLAALA RALDAPYIAL
PRADAHKLSN VLGAAMGD
