ID F8TEQ9_9CLOT Unreviewed; 708 AA.
AC F8TEQ9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=CO-methylating acetyl-CoA synthase {ECO:0000256|ARBA:ARBA00012244};
DE EC=2.3.1.169 {ECO:0000256|ARBA:ARBA00012244};
GN Name=acsB {ECO:0000313|EMBL:AEI90744.1};
OS Clostridium autoethanogenum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84023 {ECO:0000313|EMBL:AEI90744.1};
RN [1] {ECO:0000313|EMBL:AEI90744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AEI90744.1};
RX PubMed=21685168; DOI=10.1128/AEM.00355-11;
RA Kopke M., Mihalcea C., Liew F., Tizard J.H., Ali M.S., Conolly J.J.,
RA Al-Sinawi B., Simpson S.D.;
RT "2,3-butanediol production by acetogenic bacteria, an alternative route to
RT chemical synthesis, using industrial waste gas.";
RL Appl. Environ. Microbiol. 77:5467-5475(2011).
RN [2] {ECO:0000313|EMBL:AEI90744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AEI90744.1};
RA Koepke M., Mihalcea C., Liew F.M., Tizard J., Ali M., Conolly J.,
RA Al-Sinawi B., Simpson S.D.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HQ876031; AEI90744.1; -; Genomic_DNA.
DR RefSeq; WP_023162339.1; NZ_LITR01000001.1.
DR AlphaFoldDB; F8TEQ9; -.
DR SMR; F8TEQ9; -.
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:InterPro.
DR GO; GO:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2030; -; 1.
DR Gene3D; 3.30.1650.10; Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3; 1.
DR Gene3D; 3.40.1470.10; Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5; 1.
DR Gene3D; 3.40.970.20; Carbon monoxide dehydrogenase alpha subunit. Chain D, domain 4; 1.
DR Gene3D; 1.10.8.190; Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1; 1.
DR InterPro; IPR045822; ACS_CODH_B_C.
DR InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu.
DR InterPro; IPR038571; CO_DH/Ac-CoA_synth_bsu_3_sf.
DR InterPro; IPR041350; CODH_A_N.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR NCBIfam; TIGR00316; cdhC; 1.
DR NCBIfam; NF040764; CODH_ACS_al_bet; 1.
DR PANTHER; PTHR42281; -; 1.
DR PANTHER; PTHR42281:SF1; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT BETA 1; 1.
DR Pfam; PF19436; ACS_CODH_B_C; 1.
DR Pfam; PF03598; CdhC; 1.
DR Pfam; PF18537; CODH_A_N; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nickel {ECO:0000256|ARBA:ARBA00022596};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 20..101
FT /note="Carbon monoxide dehydrogenase subunit alpha ,N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18537"
FT DOMAIN 464..708
FT /note="CO dehydrogenase/acetyl-CoA synthase complex beta
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19436"
SQ SEQUENCE 708 AA; 76909 MW; 8B03657A0EA11CA5 CRC64;
MNLFQTVFTG SKQALAAAEG IVKQAVDEKG RDYKVAFPDT AYSLPVIFAA TGKKITNVGE
LEGALDIVRS LIVEEEMLDK LLNSGLATAV AAEIIEAAKY VLSDAPYAEP CVGFISDPII
RSLGVPLVTG DIPGVAVILG ECPDSETAAK IIKDYQSKGL LTCLVGKVID QAIEGKVKMG
LDLRVIPLGY DVTSVIHVVT IAIRAALIFG GIKGGQLNDI LKYTAERVPA FVNAFGPLSE
LVVSAGAGAI ALGFPVLTDQ VVPEVPTLLL TQKDYDKMVK TSLEARNIKI KITEIPIPVS
FAAAFEGERI RKNDMLAEFG GNKTKAWELV MCADQGEVED HKIEVIGPDI DTIDKAPGRM
PLGMLIKVSG TNMQKDFEPV LERRLHYFLN YIEGVMHVGQ RNLTWVRIGK EAFEKGFRLK
HFGEVIYAKM LDEFGSVVDK CEVTIITDPG KAEELEGKYA VPRYKERDAR LESLVDEKVD
TFYSCNLCQS FAPAHVCIVT PERLGLCGAV SWLDAKATLE LNPTGPCQAV PKEGVVDENL
GIWEKVNETV SKISQGAVTS VTLYSILQDP MTSCGCFECI TGIMPEANGV VMVNREFGAT
TPLGMTFGEL ASMTGGGVQT PGFMGHGRQF IASKKFMKGE GGLGRIVWMP KELKDFVAEK
LNKTAKELYN IDNFADMICD ETIATESEEV VKFLEEKGHP ALKMDPIM
//