ID A0A344LJA4_9PSEU Unreviewed; 650 AA.
AC A0A344LJA4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=A4R43_41540 {ECO:0000313|EMBL:AXB48128.1};
OS Amycolatopsis albispora.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB48128.1, ECO:0000313|Proteomes:UP000250434};
RN [1] {ECO:0000313|EMBL:AXB48128.1, ECO:0000313|Proteomes:UP000250434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:AXB48128.1,
RC ECO:0000313|Proteomes:UP000250434};
RA Wang H., Chen S., Wu Q.;
RT "Complete genome sequence and analysis of deep-sea sediment isolate,
RT Amycolatopsis sp. WP1.";
RL Submitted (APR-2016) 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; CP015163; AXB48128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A344LJA4; -.
DR KEGG; aab:A4R43_41540; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000250434; 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}.
FT DOMAIN 468..604
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 333..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 68396 MW; 7908E4EB96905C3A CRC64;
MRAFPFTAVV GLADLRLALV LSAVSPAIGG VLVRGEKGTA KSTMVRALAG LLPPVDVVTG
CRFSCDPAAP DPACPDGPHD SGAPAERRPA RLVELPVGAA EDRVIGSLDL ERALSEGVTG
YQPGLLAAAH RGLLYVDEVN LLHDHLVDAL LDAAAMGRAT VEREGVSVSH ASRFVLIGTM
NPEEGELRPQ LLDRFGLTVE VRTSREPSER VEVVRRRLAY EADPDGFAAR YDEAEAALAA
RIAEARRNLP AVTLDDAALL QIAEVCASFD VDGMRADIVT ARTAAAHAAW SGRTEVTTED
IRVAARLALP HRRRRNPFDA PGIDEEQLDQ ALRDAEPPTD GPDDDGPGSG APPEPAESSE
APSENQQPQS SPQGPQQTVG AGQPFRARLF TVDGTGEGAH GRRSRALTDS GRTIGVKPPS
VREGRPHLPA TVLAAAPHQR ARGRSGAGLV LRTRDLRFAL REGREGNLVL FCVDASGSMG
ARSRMGEVKA AVLSLLLDAY QRRDKVGLVT FRASAAELAL PPTISVDAAA SRLESLPTGG
RTPLAEGLLR AAEALRVESI RDPRRRPLLV VVTDGRATSG QDAVARAHAA ADLIARQGIA
SVVMDCESGR MRLGLAGELA NRLGAEHVPL GEVAADALAG AVRARTGRAA
//
