GenomeNet

Database: UniProt
Entry: H6LCN7_ACEWD
LinkDB: H6LCN7_ACEWD
Original site: H6LCN7_ACEWD 
ID   H6LCN7_ACEWD            Unreviewed;       652 AA.
AC   H6LCN7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Magnesium chelatase 67 kDa subunit ChlI {ECO:0000313|EMBL:AFA47819.1};
DE            EC=6.6.1.1 {ECO:0000313|EMBL:AFA47819.1};
GN   Name=chlI1 {ECO:0000313|EMBL:AFA47819.1};
GN   OrderedLocusNames=Awo_c10330 {ECO:0000313|EMBL:AFA47819.1};
OS   Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS   / WB1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Acetobacterium.
OX   NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA47819.1, ECO:0000313|Proteomes:UP000007177};
RN   [1] {ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RA   Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA   Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT   "Complete genome sequence of Acetobacterium woodii.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFA47819.1, ECO:0000313|Proteomes:UP000007177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC   {ECO:0000313|Proteomes:UP000007177};
RX   PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA   Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA   Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA   Gottschalk G., Muller V.;
RT   "An ancient pathway combining carbon dioxide fixation with the generation
RT   and utilization of a sodium ion gradient for ATP synthesis.";
RL   PLoS ONE 7:E33439-E33439(2012).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC       {ECO:0000256|ARBA:ARBA00005799}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002987; AFA47819.1; -; Genomic_DNA.
DR   RefSeq; WP_014355422.1; NC_016894.1.
DR   AlphaFoldDB; H6LCN7; -.
DR   STRING; 931626.Awo_c10330; -.
DR   KEGG; awo:Awo_c10330; -.
DR   eggNOG; COG1239; Bacteria.
DR   eggNOG; COG1240; Bacteria.
DR   HOGENOM; CLU_016684_6_0_9; -.
DR   OrthoDB; 9775079at2; -.
DR   Proteomes; UP000007177; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016851; F:magnesium chelatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00009; AAA; 1.
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; IPR011704; ATPase_dyneun-rel_AAA.
DR   InterPro; IPR041702; BchD/ChlD_VWA.
DR   InterPro; IPR041628; ChlI/MoxR_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR43473; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43473:SF2; MAGNESIUM-CHELATASE SUBUNIT CHLD, CHLOROPLASTIC; 1.
DR   Pfam; PF07728; AAA_5; 1.
DR   Pfam; PF17863; AAA_lid_2; 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   Chlorophyll biosynthesis {ECO:0000256|ARBA:ARBA00023171};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFA47819.1};
KW   Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007177}.
FT   DOMAIN          471..652
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          281..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..321
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..371
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  72584 MW;  2BD915087468188E CRC64;
     MNNTVFPFVA IVGQEEIKNA LIWNVVNPEI GGVLISGEKG TAKSSLARGV CKLTADTELV
     ELPLNTTEDR LLGNIDFEHA IKFGERRFEA GILKKADGNL LYVDEVNLLS DHLVKSLLEA
     ASSGENIIER EGMSYRHAAN FVLVGSMNPE EGGLRPQFLD RFGLYVEVKG EADTRVRAEI
     VRRRIDYERN PLAFEQKWQD QIVELSNRIE RAREDLSKVV VSDNAMQLAA SVVNEANCAG
     HRAELVIIET AKAIAAMDSR KMLNINDIKE AAKYALPHRI RENNDQPEAS PPPPESEEEQ
     EEQEEQEEQE EQEQEQNESG NESEEPQDRS EQTNDQADEP EENPEPESDS EMPEDPANDQ
     TEPDDDFFQC GEETLDSPEQ IFQIARWMSE TDKGTISKGS GKRSLMVTSS LQGRYVRNRC
     PVKGDIKDIA IDATLRTAAP YQRYREKNGM AIAINQSDIR VKIREKRTGN TIIFVVDASG
     SMGANKRMKA VKGAVISMLN DAYQKRDKVG MIVFKNHSAE LVLGVTRSVE LAEKKLTALP
     TGGRTPLAAG LDMAFEVVKA GKIKDKDMLP VIVLISDGRA TYSDRGKDAF EEAMKAAGRI
     RAEKIKTIVI DTDQNFIKLN LAEKLAVQMN ADRYQIEELQ ANSLMTAVAL SL
//
DBGET integrated database retrieval system