ID A0A0M2US00_9BACT Unreviewed; 446 AA.
AC A0A0M2US00;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma {ECO:0000313|EMBL:KKO18853.1};
GN ORFNames=BROFUL_02446 {ECO:0000313|EMBL:KKO18853.1};
OS Candidatus Brocadia fulgida.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Brocadia.
OX NCBI_TaxID=380242 {ECO:0000313|EMBL:KKO18853.1, ECO:0000313|Proteomes:UP000034954};
RN [1] {ECO:0000313|EMBL:KKO18853.1, ECO:0000313|Proteomes:UP000034954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KKO18853.1};
RX PubMed=24267221; DOI=10.1186/1471-2180-13-265;
RA Ferousi C., Speth D.R., Reimann J., Op den Camp H.J., Allen J.W.,
RA Keltjens J.T., Jetten M.S.;
RT "Identification of the type II cytochrome c maturation pathway in anammox
RT bacteria by comparative genomics.";
RL BMC Microbiol. 13:265-265(2013).
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:KKO18853.1}.
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DR EMBL; LAQJ01000232; KKO18853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2US00; -.
DR PATRIC; fig|380242.3.peg.3041; -.
DR Proteomes; UP000034954; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0046356; P:acetyl-CoA catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.11600; -; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR InterPro; IPR016218; AcylCoA_decarb/synth_gsu.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR PANTHER; PTHR36214; -; 1.
DR PANTHER; PTHR36214:SF3; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT GAMMA; 1.
DR Pfam; PF03599; CdhD; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF000376; AcCoA_decarb_gamma; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS51656; 4FE4S; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR000376-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000376-2};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR000376-
KW 2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000376-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000034954}.
FT DOMAIN 1..59
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 340
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
FT BINDING 346
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
FT BINDING 370..373
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
FT BINDING 433
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
SQ SEQUENCE 446 AA; 48118 MW; 391170E46925CD62 CRC64;
MALTGLDIYK LLPKTNCKKC GRPTCLAFAM QLAQKKANLS DCPDVSEEAK KVLGAAAAPP
IKLVTVGSGA RQVQVGEENV LFRHEEKFYH PTGVAVTIDD DLSEAAFNDR LKKINSLKLT
RVGTEIEIDL IAIINKSNAA DKFAEAAKKV SAGSHLNIIL SSASADNMKA ALQNCAEKRP
LIHGAGAGNC EAMAALAQEK KCPMTVTAQA LEELTDLAER AKKAGVEEII LDVGGGNPKE
VLQKLTKVRR LALKKNFRAL GFPMITFVCD EDPFQEIALA STYLLKYAGI VAVNACEPWA
IMPLLTARTN IFTDPQKPIQ VEPRLYAVGD VKDDSPILFT TNFSLTYYTV EGEVESSRVP
AYILSVDTGG TSVLTAYSGD KLNDKVVAKA MTDAQVDTKV KHKKLIIPGL VAVMSGKLQE
TLGWEILVGP REASGLPSYL KTVWKA
//
