ID A0A0Q7BU24_9ACTN Unreviewed; 663 AA.
AC A0A0Q7BU24;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=ASC77_00130 {ECO:0000313|EMBL:KQW52768.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW52768.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW52768.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW52768.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW52768.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW52768.1,
RC ECO:0000313|Proteomes:UP000051939};
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:KQW52768.1}.
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DR EMBL; LMDV01000001; KQW52768.1; -; Genomic_DNA.
DR RefSeq; WP_056147265.1; NZ_LMDV01000001.1.
DR AlphaFoldDB; A0A0Q7BU24; -.
DR STRING; 1736439.ASC77_00130; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000051939; 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; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 483..619
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 318..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..355
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 69953 MW; C3ADE7401A4B38C6 CRC64;
MPQQYPFSAV VGSDEPAGMA LALVLTTVSP DIGGVLVRGE KGTAKSTIVR ALAGVLPPID
VVAGDRFSSD PRDRGSLSPD GPFPADAPVE TRAVRLVELP VGATEDRVLG SLHLERALSE
GKAEYEPGLL ARAHRGILYV DEVNLLHDHL VDLLLDAAAM GRSTVERDGV SVEHAARFVL
VGTMNPEEGE LRPQLLDRFG LTVEVAAPRD PAQRVEVVRR RMAYDADPEG FAAAYAAEER
ALTARIEAAR ARVADVELSD EMLLRIAELC AACEVDGMRA DIVTARTAVA HAAWHGRTAV
TTEDVRAAAL LALPHRRRRN PFDAPGLDES LLDDVLGEDD PEPDPDPEPD PDPPGGGFDE
GDSAGAPSST TDGGDSAVEE VAQQPSRNPG TAESTVAPGA TYRPQLFTVR GVGTGEAGRR
SRAVTDNGRR IGSRPGGTGA LHLTETVRAA APHQRARGRT TGRLLLRADD LRIATREGQE
SNLVLFCVDA SGSMAARKRM EQVKAAILSL LLDAYQRRDK VGLVTFRGGD ADLALPPTYS
VEIAAARLEE LPAGGRTPLA EGLLEAARVL ELERVRDPRR RPLLVVVTDG RATSGSAAVE
RSRQAAGALA RAGVASLVVD CESGAMRLGL ASVLAQHLGA EHVPIAEVSA EALAGVVRHG
RAA
//
