ID   ACDA2_METKA             Reviewed;         632 AA.
AC   Q8TXF5;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Putative acetyl-CoA decarbonylase/synthase complex subunit alpha-like;
DE            Short=ACDS complex subunit alpha-like;
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha-like;
DE            Short=ACDS CODH subunit alpha-like;
GN   Name=cdhA2; OrderedLocusNames=MK0719;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC   -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC       cleavage of acetyl-CoA, allowing autotrophic growth from CO(2). The
CC       alpha-epsilon subcomponent functions as a carbon monoxide
CC       dehydrogenase. {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- CAUTION: This protein lacks several conserved Cys residues that bind
CC       [4Fe-4S] clusters in other CODHs. Therefore, it is not clear whether
CC       this protein is active. However, the protein would be able to bind a
CC       [Ni-4Fe-4S] cluster, which is the active site of CO oxidation.
CC       {ECO:0000305}.
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DR   EMBL; AE009439; AAM01933.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TXF5; -.
DR   SMR; Q8TXF5; -.
DR   STRING; 190192.MK0719; -.
DR   EnsemblBacteria; AAM01933; AAM01933; MK0719.
DR   KEGG; mka:MK0719; -.
DR   PATRIC; fig|190192.8.peg.760; -.
DR   HOGENOM; CLU_361186_0_0_2; -.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.2030; -; 2.
DR   InterPro; IPR004137; HCP/CODH.
DR   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR30109; PTHR30109; 2.
DR   Pfam; PF03063; Prismane; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Nickel; Reference proteome.
FT   CHAIN           1..632
FT                   /note="Putative acetyl-CoA decarbonylase/synthase complex
FT                   subunit alpha-like"
FT                   /id="PRO_0000155079"
FT   BINDING         200
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         226
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000305"
FT   BINDING         263
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         379
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         408
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT   BINDING         438
FT                   /ligand="[Ni-4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:47739"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ   SEQUENCE   632 AA;  68559 MW;  722B7DCE1C510A08 CRC64;
     MGIEWEGVKV EIGELVVEGD SESEMEGPTR RELLPWDRTL ASVYDLAVVP GDSEEERREV
     ARTIVTLCCE GTAGLISTAR LVVELLRQTG ENLDPGFDAE TPLPLYETLL GSSPECADDL
     EAGLSYAERE LTSSVSELLR SHSLKGYESV AMHAGAIGLL AMEIADATPS TLMEVTESEE
     VFEIGTDDLP RRPTVLLVGH LPLLGHIITE ELGTLARQVE LVGLTHTAWP NREDHVRVVG
     PLSMYHEYLS SGFADVVVVD GACPGEDVIE AAREGGSKLV ATVGARVADL LDVTDYPVEE
     AVEVLVTEED AVYVEEPIKA VEIAAWAALR VEGSRDRREP PRRAFRVGPP TRLTDVVIRN
     VGVPVVAGNI PGIVVLVSCP EKSADVEEPA KIAEVLLERG YLVLVPGCLA VALGSYLDDD
     GKTLYERYPD TLLNTGPCTS AAHLVGACIR VGVIFGKLPI RGEFVRVADY VLNRVGACVI
     AWGGEYSEHL VSAAYGVTRW GIPVVLGPDP EAGSLLVEKN PKVIDACSGE EVEDPTPEHL
     RCVVSDWKEA AITAARLCMR PNDTPEGRQN KVESYVELYR ELYGELPPDL DLLIRDESDI
     PVTLRSEIRE LLEETGWTPR SRASDPTLLP EG