ID D4S4J6_9FIRM Unreviewed; 343 AA.
AC D4S4J6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN ORFNames=HMPREF7545_0461 {ECO:0000313|EMBL:EFF66832.1};
OS Selenomonas noxia ATCC 43541.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF66832.1, ECO:0000313|Proteomes:UP000003701};
RN [1] {ECO:0000313|EMBL:EFF66832.1, ECO:0000313|Proteomes:UP000003701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF66832.1,
RC ECO:0000313|Proteomes:UP000003701};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2010) 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:EFF66832.1}.
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DR EMBL; ACKT01000013; EFF66832.1; -; Genomic_DNA.
DR RefSeq; WP_006695457.1; NZ_GG749282.1.
DR AlphaFoldDB; D4S4J6; -.
DR eggNOG; COG1239; Bacteria.
DR HOGENOM; CLU_016684_0_2_9; -.
DR InParanoid; D4S4J6; -.
DR OrthoDB; 9775079at2; -.
DR Proteomes; UP000003701; 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 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 30..213
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 343 AA; 37185 MW; 2ACDBDE4BB4E4F29 CRC64;
MKTKAVYPFT AIVGQEEMKK ALLLSVVMPS LGGVLIKGEK GTAKSTAVRA TAALLPNLRA
VTGCACHCDP SLPDLYCDAC RARRGFGEEL TAEEVPMRVV ELPVSATEDR VVGTLDMEAA
IQHGRKEFEP GILAAANRNI LYVDEINLLE DHIVDILLDS AAMGVNTVER EGISYAHPAR
FVLVGTMNPE EGDIRPQLLD RFALSVTVAG ECEAETRVEV IRRRIAYERD PDAFAEAYAG
AQQELREQIT AARARVPHVE VPDEILGYAA QISLTLGVDG HRADITLIKA GIAHAALAGR
MAVTAEDLQR VSRLVLAHRM RRRPFEEGAV DWSAVDAILG ESA
//
