ID X1MUH2_9ZZZZ Unreviewed; 304 AA.
AC X1MUH2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=CO-methylating acetyl-CoA synthase {ECO:0000256|ARBA:ARBA00012244};
DE EC=2.3.1.169 {ECO:0000256|ARBA:ARBA00012244};
DE Flags: Fragment;
GN ORFNames=S06H3_25466 {ECO:0000313|EMBL:GAI21676.1};
OS marine sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAI21676.1};
RN [1] {ECO:0000313|EMBL:GAI21676.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAI21676.1};
RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA Takami H.;
RT "High frequency of phylogenetically diverse reductive dehalogenase-
RT homologous genes in deep subseafloor sedimentary metagenomes.";
RL Front. Microbiol. 5:80-80(2014).
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:GAI21676.1}.
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; BARV01014659; GAI21676.1; -; Genomic_DNA.
DR AlphaFoldDB; X1MUH2; -.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu.
DR InterPro; IPR038571; CO_DH/Ac-CoA_synth_bsu_3_sf.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR PANTHER; PTHR42281; -; 1.
DR PANTHER; PTHR42281:SF1; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT BETA 1; 1.
DR Pfam; PF03598; CdhC; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAI21676.1"
FT NON_TER 304
FT /evidence="ECO:0000313|EMBL:GAI21676.1"
SQ SEQUENCE 304 AA; 34113 MW; 760975713EFF18B0 CRC64;
EGGVQLGWET RLVPFGREIT SAIYALGFAS RAALSFGGVQ AGDFRHNLLY NKNRIFAFVM
ALGEVTDEWY ATAAGAINYG FPVIADSDIP EILPTGVCTY EHVVSNIPHD QIVEKSIEVR
GLKVKITEIP IPVSVSPAFE GERIRKEEMH CEFGGQRTPA FEWLRMRDIS EVEDAGVEVL
GPDSDSLEPG GKLPLGIIVE VAGRKMQRDF EPVLERHIHT FMNEAQGLWH MGQRDINWVR
ISNNAAKAGF KLEHIGKLLH AKFHDEYSSI LDKVQVKLFT DQKQVEELRK QAQAVYAERD
ARLE
//