ID Q47T66_THEFY Unreviewed; 673 AA.
AC Q47T66;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN OrderedLocusNames=Tfu_0313 {ECO:0000313|EMBL:AAZ54351.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54351.1};
RN [1] {ECO:0000313|EMBL:AAZ54351.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ54351.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) 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; CP000088; AAZ54351.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47T66; -.
DR STRING; 269800.Tfu_0313; -.
DR KEGG; tfu:Tfu_0313; -.
DR eggNOG; COG1239; Bacteria.
DR eggNOG; COG1240; Bacteria.
DR HOGENOM; CLU_016684_6_0_11; -.
DR OrthoDB; 9775079at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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 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 Ligase {ECO:0000313|EMBL:AAZ54351.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 491..627
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 318..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 70594 MW; 133653B5B7655F73 CRC64;
MEERVHVYPF SAIVGSDDLV LALILTGISP DIGGVLIRGE KGTAKSTAVR AQAALLPPIT
VVTDCRFSCD PAAPDPDCPD GPHPPSVASA TRPVRLVELP VGAGEDRVVG SLHLEKALSG
SGVEYEPGLL ARANRGILYV DEVNLLHDHL VDLLLDAAAM GRATVERDGV SLSHAARFTL
VGTMNPEEGE LRPQLLDRFG LSVEVAAPRD PAVRAEIIRR RLAFDADPAG FTSAYATAEQ
QLAERIADAR LRLPKVVLGQ EALLAIAEVC AAFDVDGMRA DLVCARAAVA HAAWCGRTDV
TRADVRAAAR LALPHRRRRT PFDSPGMDEG LLDEILGEDH DPDPGPDGSG GPGGPPSDSG
SDTPPPTAGS TPDPPASGLG SPTSSNDDPR PDAPAPVSVT APEEPYRPRL FTVAGTGKGT
LGRRSRAITT SGRTVGDVPA GRGTGPIHLA ATVRTAALRH ATSRSSPDTT RLSIALSDLR
RSLCEGKESN LVLLCVDASG SMAARRRMSQ VKTAVLALLL DAYRRRDRVG LITFRNHEAT
LTLPPTGSVD VAAARLRELP AGGRTPLAEG LLKAAETLRR ERLRDPDRRA LLVVVTDGRA
TAGPKAVERS LHAADHLARE GVSALVIDSE TGRFRMGLAA ALARRMGAEY VHVGEVSAEA
ITSAVAGATT RAA
//
