ID A0A0N0SDN5_9ACTN Unreviewed; 712 AA.
AC A0A0N0SDN5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=ADK51_14535 {ECO:0000313|EMBL:KOU26118.1};
OS Streptomyces sp. WM6368.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415554 {ECO:0000313|EMBL:KOU26118.1, ECO:0000313|Proteomes:UP000037718};
RN [1] {ECO:0000313|EMBL:KOU26118.1, ECO:0000313|Proteomes:UP000037718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6368 {ECO:0000313|EMBL:KOU26118.1,
RC ECO:0000313|Proteomes:UP000037718};
RA Noorani M.;
RL Submitted (JUL-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:KOU26118.1}.
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DR EMBL; LGDA01000172; KOU26118.1; -; Genomic_DNA.
DR RefSeq; WP_053702763.1; NZ_LGDA01000172.1.
DR AlphaFoldDB; A0A0N0SDN5; -.
DR PATRIC; fig|1415554.3.peg.3056; -.
DR Proteomes; UP000037718; 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; 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 510..654
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 335..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 74634 MW; E831E7F215FD7ADF CRC64;
MSTPYPFTAV VGQSDLRLAL LLNAVSPAVG GVLVRGEKGT AKSTAVRALS ALLPKVDVVS
GCRFSCAPTG PDPACPDGPH EPGPGALRPA RMVELPVGAS EDRLVGALDI ERALAEGVKA
FEPGLLADAH RGILYVDEVN LLHDHLIDLL LDAAAMGASY VEREGVSVRH AARFLLVGTM
NPEEGELRPQ LLDRFGLTVE VAASREPAQR VEVVRRRLAY EDDPAGFATR WAGDEHEVRA
RVVAARALLP KVSLGDTALL QIAATCAGFE VDGMRADIVM ARTATALAAW AGRTEVRKED
VRQAALLALP HRRRRNPFDA PGLDEDMLDR ILDEFPDEEP EPDPEPEPQG PDDGGPEDGG
PDGGPGDTPP QGGGPDTPGT ERQPESDSAD APQSPESPES PQSPEPQPSA QESTGPEQAA
VRAAEPFRTK MLSVPGLGEG ASGRRSRART AHGRTTGAQR PRGHLTKLHL AATIQAAAPH
QKARGRSGRG LVIRKDDLRQ ASREGREGNL VLFVVDASGS MAARQRMGAV KGAVLSLLLD
AYQRRDKVGL ITFRGATAEL ALPPTSSVDA AAARLEQLPT GGRTPLAAGL LKAHEVLRIE
RLRDPSRRPL LVVVTDGRAT SAGNAGGRTD STPRELAGHS ARLLQAGGVA SVVVDCESGP
VRLGLAGVLA RDLGGPAVTL DGLRADSLAG LVKNVRTAVA ATASPNSNRR AA
//
