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Database: UniProt
Entry: Q46G04
LinkDB: Q46G04
Original site: Q46G04 
ID   ACDA1_METBF             Reviewed;         806 AA.
AC   Q46G04;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   10-APR-2019, entry version 111.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            EC=1.2.7.4 {ECO:0000255|HAMAP-Rule:MF_01137};
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   OrderedLocusNames=Mbar_A0204 {ECO:0000312|EMBL:AAZ69188.1};
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT,
RP   INDUCTION, AND PATHWAY.
RC   STRAIN=MS;
RX   PubMed=6425262;
RA   Krzycki J.A., Zeikus J.G.;
RT   "Characterization and purification of carbon monoxide dehydrogenase
RT   from Methanosarcina barkeri.";
RL   J. Bacteriol. 158:231-237(1984).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACDS EPSILON
RP   SUBUNIT; IRON-SULFUR (4FE-4S); NICKEL-IRON-SULFUR (NI-4FE-4S) AND
RP   CARBON MONOXIDE, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX   PubMed=18621675; DOI=10.1073/pnas.0800415105;
RA   Gong W., Hao B., Wei Z., Ferguson D.J., Tallant T., Krzycki J.A.,
RA   Chan M.K.;
RT   "Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase
RT   component of the Methanosarcina barkeri acetyl-CoA
RT   decarbonylase/synthase complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9558-9563(2008).
CC   -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC       cleavage of acetyl-CoA, allowing growth on acetate as sole source
CC       of carbon and energy. The alpha-epsilon subcomponent functions as
CC       a carbon monoxide dehydrogenase. {ECO:0000255|HAMAP-Rule:MF_01137,
CC       ECO:0000269|PubMed:6425262}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2
CC         H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137,
CC         ECO:0000269|PubMed:18621675};
CC       Note=Binds 7 [4Fe-4S] clusters per heterotetramer.
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675};
CC   -!- COFACTOR:
CC       Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137,
CC         ECO:0000269|PubMed:18621675};
CC       Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000269|PubMed:18621675};
CC   -!- ACTIVITY REGULATION: Carbon monoxide dehydrogenase activity is
CC       inhibited by KCN and is rapidly inactivated by O(2).
CC       {ECO:0000269|PubMed:6425262}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 mM for CO (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:6425262};
CC         Vmax=1300 umol/min/mg enzyme for CO dehydrogenase activity using
CC         methyl viologen as electron acceptor (at 37 degrees Celsius)
CC         {ECO:0000269|PubMed:6425262};
CC   -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000305|PubMed:6425262}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits
CC       (PubMed:6425262). The ACDS complex is made up of alpha, epsilon,
CC       beta, gamma and delta subunits with a probable stoichiometry of
CC       (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By
CC       similarity). {ECO:0000255|HAMAP-Rule:MF_01137,
CC       ECO:0000269|PubMed:6425262, ECO:0000305|PubMed:18621675}.
CC   -!- INDUCTION: Up-regulated during growth on acetate.
CC       {ECO:0000269|PubMed:6425262}.
CC   -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster;
CC       cluster C is a mixed Ni-Fe-S cluster which is the active site of
CC       CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S
CC       cluster that bridges the two subunits of the CODH dimer. Contains
CC       two additional 4Fe-4S clusters, dubbed E and F, that probably
CC       transport electrons from ferredoxin to the B cluster.
CC       {ECO:0000255|HAMAP-Rule:MF_01137, ECO:0000305|PubMed:18621675}.
CC   -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01137}.
DR   EMBL; CP000099; AAZ69188.1; -; Genomic_DNA.
DR   RefSeq; WP_011305243.1; NC_007355.1.
DR   PDB; 3CF4; X-ray; 2.00 A; A=1-806.
DR   PDBsum; 3CF4; -.
DR   ProteinModelPortal; Q46G04; -.
DR   SMR; Q46G04; -.
DR   STRING; 269797.Mbar_A0204; -.
DR   EnsemblBacteria; AAZ69188; AAZ69188; Mbar_A0204.
DR   GeneID; 3626295; -.
DR   KEGG; mba:Mbar_A0204; -.
DR   eggNOG; arCOG02428; Archaea.
DR   eggNOG; COG1152; LUCA.
DR   HOGENOM; HOG000224351; -.
DR   KO; K00192; -.
DR   OMA; EVCGICC; -.
DR   OrthoDB; 1404at2157; -.
DR   UniPathway; UPA00642; -.
DR   EvolutionaryTrace; Q46G04; -.
DR   Proteomes; UP000008156; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR   CDD; cd01916; ACS_1; 1.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.40.50.2030; -; 2.
DR   HAMAP; MF_01137; CdhA; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004460; CDHA.
DR   InterPro; IPR004137; HCP/CODH.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR30109; PTHR30109; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF03063; Prismane; 2.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00314; cdhA; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Complete proteome; Iron; Iron-sulfur;
KW   Metal-binding; Methanogenesis; Nickel; Oxidoreductase; Repeat.
FT   CHAIN         1    806       Acetyl-CoA decarbonylase/synthase complex
FT                                subunit alpha 1.
FT                                /FTId=PRO_0000436851.
FT   DOMAIN      407    436       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   DOMAIN      446    475       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        73     73       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL        76     76       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL        77     77       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL        79     79       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL        84     84       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL        94     94       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       250    250       Nickel-iron-sulfur (Ni-4Fe-4S); via tele
FT                                nitrogen. {ECO:0000269|PubMed:18621675}.
FT   METAL       278    278       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000269|PubMed:18621675}.
FT   METAL       323    323       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       417    417       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       420    420       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       423    423       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       427    427       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       455    455       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       458    458       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       461    461       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       465    465       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000244|PDB:3CF4, ECO:0000255|HAMAP-
FT                                Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       523    523       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       552    552       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   METAL       587    587       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137,
FT                                ECO:0000269|PubMed:18621675}.
FT   BINDING     117    117       Carbon monoxide; via tele nitrogen.
FT                                {ECO:0000269|PubMed:18621675}.
FT   TURN         50     57       {ECO:0000244|PDB:3CF4}.
FT   HELIX        58     64       {ECO:0000244|PDB:3CF4}.
FT   STRAND       65     69       {ECO:0000244|PDB:3CF4}.
FT   STRAND       72     76       {ECO:0000244|PDB:3CF4}.
FT   TURN         87     89       {ECO:0000244|PDB:3CF4}.
FT   HELIX        98    132       {ECO:0000244|PDB:3CF4}.
FT   HELIX       148    154       {ECO:0000244|PDB:3CF4}.
FT   HELIX       162    164       {ECO:0000244|PDB:3CF4}.
FT   HELIX       165    180       {ECO:0000244|PDB:3CF4}.
FT   HELIX       190    218       {ECO:0000244|PDB:3CF4}.
FT   STRAND      230    234       {ECO:0000244|PDB:3CF4}.
FT   HELIX       235    237       {ECO:0000244|PDB:3CF4}.
FT   STRAND      244    250       {ECO:0000244|PDB:3CF4}.
FT   HELIX       253    264       {ECO:0000244|PDB:3CF4}.
FT   TURN        268    270       {ECO:0000244|PDB:3CF4}.
FT   STRAND      271    277       {ECO:0000244|PDB:3CF4}.
FT   HELIX       278    283       {ECO:0000244|PDB:3CF4}.
FT   TURN        284    287       {ECO:0000244|PDB:3CF4}.
FT   STRAND      296    301       {ECO:0000244|PDB:3CF4}.
FT   HELIX       302    304       {ECO:0000244|PDB:3CF4}.
FT   HELIX       305    311       {ECO:0000244|PDB:3CF4}.
FT   STRAND      315    319       {ECO:0000244|PDB:3CF4}.
FT   STRAND      321    323       {ECO:0000244|PDB:3CF4}.
FT   HELIX       328    334       {ECO:0000244|PDB:3CF4}.
FT   STRAND      339    341       {ECO:0000244|PDB:3CF4}.
FT   HELIX       358    366       {ECO:0000244|PDB:3CF4}.
FT   STRAND      369    374       {ECO:0000244|PDB:3CF4}.
FT   HELIX       378    398       {ECO:0000244|PDB:3CF4}.
FT   HELIX       407    416       {ECO:0000244|PDB:3CF4}.
FT   HELIX       422    426       {ECO:0000244|PDB:3CF4}.
FT   HELIX       433    441       {ECO:0000244|PDB:3CF4}.
FT   HELIX       446    454       {ECO:0000244|PDB:3CF4}.
FT   HELIX       460    464       {ECO:0000244|PDB:3CF4}.
FT   HELIX       471    478       {ECO:0000244|PDB:3CF4}.
FT   HELIX       480    484       {ECO:0000244|PDB:3CF4}.
FT   STRAND      488    491       {ECO:0000244|PDB:3CF4}.
FT   HELIX       499    511       {ECO:0000244|PDB:3CF4}.
FT   STRAND      512    514       {ECO:0000244|PDB:3CF4}.
FT   STRAND      517    520       {ECO:0000244|PDB:3CF4}.
FT   HELIX       532    542       {ECO:0000244|PDB:3CF4}.
FT   STRAND      546    550       {ECO:0000244|PDB:3CF4}.
FT   HELIX       551    557       {ECO:0000244|PDB:3CF4}.
FT   HELIX       568    571       {ECO:0000244|PDB:3CF4}.
FT   STRAND      575    577       {ECO:0000244|PDB:3CF4}.
FT   STRAND      581    586       {ECO:0000244|PDB:3CF4}.
FT   HELIX       587    590       {ECO:0000244|PDB:3CF4}.
FT   HELIX       591    603       {ECO:0000244|PDB:3CF4}.
FT   HELIX       613    623       {ECO:0000244|PDB:3CF4}.
FT   STRAND      626    630       {ECO:0000244|PDB:3CF4}.
FT   HELIX       636    647       {ECO:0000244|PDB:3CF4}.
FT   STRAND      652    654       {ECO:0000244|PDB:3CF4}.
FT   HELIX       656    661       {ECO:0000244|PDB:3CF4}.
FT   STRAND      662    666       {ECO:0000244|PDB:3CF4}.
FT   HELIX       672    674       {ECO:0000244|PDB:3CF4}.
FT   STRAND      675    679       {ECO:0000244|PDB:3CF4}.
FT   TURN        680    682       {ECO:0000244|PDB:3CF4}.
FT   STRAND      685    687       {ECO:0000244|PDB:3CF4}.
FT   STRAND      692    698       {ECO:0000244|PDB:3CF4}.
FT   HELIX       702    712       {ECO:0000244|PDB:3CF4}.
FT   HELIX       720    737       {ECO:0000244|PDB:3CF4}.
FT   HELIX       745    748       {ECO:0000244|PDB:3CF4}.
FT   HELIX       752    754       {ECO:0000244|PDB:3CF4}.
FT   HELIX       760    771       {ECO:0000244|PDB:3CF4}.
FT   STRAND      774    776       {ECO:0000244|PDB:3CF4}.
FT   TURN        777    780       {ECO:0000244|PDB:3CF4}.
FT   STRAND      781    784       {ECO:0000244|PDB:3CF4}.
FT   STRAND      796    798       {ECO:0000244|PDB:3CF4}.
FT   HELIX       800    802       {ECO:0000244|PDB:3CF4}.
SQ   SEQUENCE   806 AA;  88775 MW;  25620ACDA618E9CA CRC64;
     MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKAKELV NAGPTLFAGL ESYRDDWNFK
     LLDRYEPVIT PMCDQCCYCT YGPCDLSGNK RGACGIDMLG HNGREFFLRV ITGTACHAAH
     GRHLLDHLIE TFGEDLPLNL GQSNVLTPNI TISTGLSPKT LGEVKPAMEY VEEQLTQLLA
     TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDIVQVTAYD FPRADPEAPL IEIGMGTIDK
     SKPFLCVIGH NVAGVTYMMD YMEDHDLTDK MEIAGLCCTA IDLTRYKEAD RRPPYAKVIG
     SMSKELKVIR SGMPDVIVVD EQCVRGDIVP EAQKLMIPVI ASNPKIMYGL PNRTDADVDE
     TIEELRSGKI PGCVMLDYDK LGEICIRLTM EMAPIRDASG ITAIPTDEEF TNWVMKCADC
     GACMIACPEE LDIPEAMGFA KEGDYSYLDI LHDQCIGCRR CEQVCKKEIP ILNIIEKAAQ
     KQISEEKGLM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYPEGT KDVYYIAEEF
     LKRNFIVVTT GCGAMDIGMF KDEDGKTLYE RFPGGFECGG LANIGSCVSN AHITGAAEKV
     AAIFAQRTLE GNLAEIGDYV LNRVGACGLA WGAFSQKASS IGTGCNILGI PAVLGPHSSK
     YRRALIAKNY EEDKWKVYDA RNGQEMAIPP APEFLLTTAE TWQEAIPMMA KACIRPSDNN
     MGRSIKLTHW MELHKKYLGS KPEDWWKFVR NEADLPLATR EALLKELEKE HGWEIDWKRK
     KVISGPKIKF DVSAQPTNLK RLCKEA
//
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