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Database: UniProt
Entry: A0A151FBA2_9EURY
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Original site: A0A151FBA2_9EURY 
ID   A0A151FBA2_9EURY        Unreviewed;       382 AA.
AC   A0A151FBA2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit delta {ECO:0000256|HAMAP-Rule:MF_01135};
DE            Short=ACDS complex subunit delta {ECO:0000256|HAMAP-Rule:MF_01135};
DE   AltName: Full=Corrinoid/iron-sulfur component small subunit {ECO:0000256|HAMAP-Rule:MF_01135};
GN   Name=cdhD {ECO:0000256|HAMAP-Rule:MF_01135};
GN   ORFNames=AYK18_01025 {ECO:0000313|EMBL:KYK38164.1};
OS   Theionarchaea archaeon DG-70.
OC   Archaea; Euryarchaeota; Theionarchaea.
OX   NCBI_TaxID=1803813 {ECO:0000313|EMBL:KYK38164.1, ECO:0000313|Proteomes:UP000075311};
RN   [1] {ECO:0000313|Proteomes:UP000075311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC       acetyl-CoA, allowing autotrophic growth from CO(2). Probably maintains
CC       the overall quaternary structure of the ACDS complex.
CC       {ECO:0000256|HAMAP-Rule:MF_01135}.
CC   -!- SUBUNIT: Heterodimer of delta and gamma chains. The ACDS complex is
CC       made up of alpha, epsilon, beta, gamma and delta chains with a probable
CC       stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
CC       {ECO:0000256|HAMAP-Rule:MF_01135}.
CC   -!- SIMILARITY: Belongs to the CdhD family. {ECO:0000256|HAMAP-
CC       Rule:MF_01135}.
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:KYK38164.1}.
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DR   EMBL; LSSB01000035; KYK38164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151FBA2; -.
DR   Proteomes; UP000075311; Unassembled WGS sequence.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR   HAMAP; MF_01135; CdhD; 1.
DR   InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR   InterPro; IPR004486; CO_DH/Ac-CoA_synth_dsu.
DR   InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR   NCBIfam; TIGR00381; cdhD; 1.
DR   PANTHER; PTHR36214; -; 1.
DR   PANTHER; PTHR36214:SF5; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT DELTA; 1.
DR   Pfam; PF03599; CdhD; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          73..311
FT                   /note="CO dehydrogenase/acetyl-CoA synthase delta subunit
FT                   TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF03599"
SQ   SEQUENCE   382 AA;  42666 MW;  E05D073D7191D22B CRC64;
     MDIDRLIRML EDTDEIELEN VDIFAEELEL LMSPIGKAMK PAEYRELQYE PPLEEYRGEI
     PVVKFGHTKS EGGTRSHSLY VGGEKTMPFY RFEHENPYKP VVAFDVFDMK IGLAKPVKVH
     YKEVLEDPAA WAKLSVDKFG ADMVTIHLIS TDPLLKDTPV SDAVKTVEEV LQAVKVPIII
     GGSGNPGKDP EVLEKAAEVA EGERVMLNSA SMNLDYKRVA QAAMDYGHVV LSWTQLDIND
     QKTLNRHLFD MGVQPENMLI DPTTAALGYG LEYSFSMMER MRLAGLKGDT DLQCPIASGT
     TNAWGAREAW MKESPIEGET WGDRMKRGPL WEAVSAFTLC LAGCDLFMMM CPTSVQLFRE
     MTTQLTEDHE VNSAADWLTG GA
//
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