ID I3IP88_9BACT Unreviewed; 446 AA.
AC I3IP88;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma {ECO:0000313|EMBL:GAB63533.1};
GN ORFNames=KSU1_D0224 {ECO:0000313|EMBL:GAB63533.1};
OS Candidatus Jettenia caeni.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Brocadiaceae; Candidatus Jettenia.
OX NCBI_TaxID=247490 {ECO:0000313|EMBL:GAB63533.1, ECO:0000313|Proteomes:UP000002985};
RN [1] {ECO:0000313|EMBL:GAB63533.1, ECO:0000313|Proteomes:UP000002985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22673575; DOI=10.1016/j.febslet.2012.04.041;
RA Hira D., Toh H., Migita C.T., Okubo H., Nishiyama T., Hattori M.,
RA Furukawa K., Fujii T.;
RT "Anammox organism KSU-1 expresses a NirK-type copper-containing nitrite
RT reductase instead of a NirS-type with cytochrome cd1.";
RL FEBS Lett. 586:1658-1663(2012).
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:GAB63533.1}.
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DR EMBL; BAFH01000004; GAB63533.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IP88; -.
DR STRING; 247490.KSU1_D0224; -.
DR eggNOG; COG1456; Bacteria.
DR OrthoDB; 140437at2; -.
DR Proteomes; UP000002985; 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:UP000002985}.
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; 48404 MW; C9770564E3171569 CRC64;
MALTGLDIYK LLPKTNCKKC GRPTCLAFAM QLAQKKANLS DCPDVSEEAK RVLGAASAPP
IKLVTVGTGA RKVEIGEENV LFRHEEKFYH PTGIAVTIHD DLDDAAFDNR LKKINNLKMS
RVGTEIEIDL VAIINKSASA EKFADAAKKV SDGSHLNIIL SSTSVDNMKA ALANCAEKRP
LIHGANAGNC ESMAALAKEK NCPMTVTAPT LEELADLAER VKKVGVEEIV LDVSGDKPKE
VLQKLTRIRR AALKKNFRAL GFPMITFACD DDAFQEISMA STYLVKYAGI VVVNTCESWG
IMPLLTVRTN IFTDPQKPIQ VEPKLYAVGD AKEDSPVLFT TNFSLTYYTV EGEVEGSRIP
AFILSVDTGG TSVLTAYSGD KLNDKVVAKA MADAQVETKV KHRKLIIPGL VAVMSGKLQE
TLGWEIMVGP REASGLASYL KTVWKP
//
