ID A0A1Z1W836_9ACTN Unreviewed; 671 AA.
AC A0A1Z1W836;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN Name=chlD {ECO:0000313|EMBL:ARX82585.1};
GN ORFNames=SMD44_01998 {ECO:0000313|EMBL:ARX82585.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX82585.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX82585.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX82585.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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DR EMBL; CP021748; ARX82585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z1W836; -.
DR STRING; 67267.GCA_000716675_04943; -.
DR KEGG; salf:SMD44_01998; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000195880; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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; TIGR02442; Cob-chelat-sub; 1.
DR PANTHER; PTHR35023; CHELATASE-RELATED; 1.
DR PANTHER; PTHR35023:SF1; MG-PROTOPORPHYRIN IX CHELATASE; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000195880}.
FT DOMAIN 483..660
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 334..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 70122 MW; CACCEF54C8581AD6 CRC64;
MSTPYPFTAL VGQDDLRLAL LLNAVSPAVG GVLVRGEKGT AKSTAVRALS ALLPEVDVVP
GCRFSCAPGA PDPSCPDGPH EAGGGVARAA RMVELPVGAS EDRLVGALDI ERALAEGVKA
FEPGLLADAH RGILYVDEVN LLHDHLVDLL LDAAAMGASY VEREGVSVRH AARFLLVGTM
NPEEGELRPQ LLDRFGLTVE VSASREPDQR VEVVRRRLAY DDDPDGFAAR WGDEEGAVRG
RIVAARALLP RVRLGDGALR QIAATCAAFE VDGMRADIVM ARTATALAAW AGREDVLAED
VRQAALLALP HRRRRNPFDA PGLDEDKLDE TLEEFGENDG DDEPDPDGGG PDGGGGQPPQ
DSGPEQSGDG AAATPEAADD GQPGAGGAGE QQAVRAGEPF RTKVLSVPGL GEGAAGRRSR
ARTEHGRTTG ARRPRGALTK LHLAATVQAA APHQRARGRS GRGLVVRRDD LRQATREGRE
GNLVLFVVDA SGSMAARQRM SAVKGAVLSL LLDAYQRRDK VGLVTFRGSG AEVALPPTSS
VDAAAVRLES LPTGGRTPIA AGLLRAHEVL RVERLRDPAR RPLVIVVTDG RATGGVEPVA
QAGRAARLFA AEGQASVVVD CESGPVRLGL AGQLAGELGG TAVTLDELRA DSIAGLVKDV
RESYGSARRV A
//
