ID A0A0T1Q9U7_9ACTN Unreviewed; 691 AA.
AC A0A0T1Q9U7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=ASC82_12555 {ECO:0000313|EMBL:KQX13393.1};
OS Streptomyces sp. Root431.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736535 {ECO:0000313|EMBL:KQX13393.1, ECO:0000313|Proteomes:UP000051818};
RN [1] {ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|Proteomes:UP000051818};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX13393.1, ECO:0000313|Proteomes:UP000051818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root431 {ECO:0000313|EMBL:KQX13393.1,
RC ECO:0000313|Proteomes:UP000051818};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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:KQX13393.1}.
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DR EMBL; LMEI01000008; KQX13393.1; -; Genomic_DNA.
DR RefSeq; WP_056646163.1; NZ_LMEI01000008.1.
DR AlphaFoldDB; A0A0T1Q9U7; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000051818; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
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}.
FT DOMAIN 503..681
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 336..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 72038 MW; CA06927E0BEA65F1 CRC64;
MSTRYPFTAV VGMDDLRLAL LLNAVSPAVG GVLVRGEKGT AKSTAVRALA DLLPVVPVVA
GCRFSCDPVS PDPGCPDGPH ADAPGAERAA RMVELPVGAS EDRLVGSLDI EKALSEGVKA
FEPGLLAAAH RGILYVDEVN LLSDHLIDHL LDAAAMGASH VEREGVSVRH AARFLLVGTM
NPEEGELRPQ LLDRFGLTVE VAASRVPEQR VEVVRRRLAF EDDPAVFAAL WADEETALRD
RIVAARTLLP KVVLGDAALL QIAATCAAFE VDGMRADIVM ARAATALAAW AGRTEVTSED
VRQAALLALP HRRRRNPFDA PGLDEDKLDE TLEQFKGEEP QPDPDEDPEP DGPGDGGPGD
GGPDGGGPGG GIPPQGEGPA PETDGVPEET PAEAPAPAPA PQAQGPGAGE RAAVQAAEPF
RTKMLSVPGL GQGAAGRRSR ARTEHGRTTG ATRPRGALTK LHLAATVQAA APHQRARGRT
GPGLVVRRDD LRQATREGRE GNLVLFAVDA SGSMAARQRM SAVKGAVLSL LLDAYQRRDK
VGLITFRGRT AELALPPTSS VDAAAARLEQ LPTGGRTPLS AGLLKAHDVL RIERLRDPSR
RPLLVVVTDG RATGGGADPV ALAARAAQLH AAEGTASVVV DCETGPVRLG LAGSLARELG
GTAVTLDELR ADSIAGLVRD VQAEQTTRRA A
//