ID Q8TN86_METAC Unreviewed; 296 AA.
AC Q8TN86;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Pyruvate synthase, beta subunit {ECO:0000313|EMBL:AAM05793.1};
GN Name=porB {ECO:0000313|EMBL:AAM05793.1};
GN OrderedLocusNames=MA_2407 {ECO:0000313|EMBL:AAM05793.1};
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937 {ECO:0000313|EMBL:AAM05793.1, ECO:0000313|Proteomes:UP000002487};
RN [1] {ECO:0000313|EMBL:AAM05793.1, ECO:0000313|Proteomes:UP000002487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC {ECO:0000313|Proteomes:UP000002487};
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A., Hedderich R., Ingram-Smith C.,
RA Kuettner C.H., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B.,
RA Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H.,
RA de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L.,
RA Paulsen I., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H.,
RA Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain. {ECO:0000256|ARBA:ARBA00011595}.
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DR EMBL; AE010299; AAM05793.1; -; Genomic_DNA.
DR RefSeq; WP_011022378.1; NC_003552.1.
DR AlphaFoldDB; Q8TN86; -.
DR STRING; 188937.MA_2407; -.
DR EnsemblBacteria; AAM05793; AAM05793; MA_2407.
DR GeneID; 1474296; -.
DR KEGG; mac:MA_2407; -.
DR HOGENOM; CLU_058423_0_0_2; -.
DR InParanoid; Q8TN86; -.
DR OrthoDB; 296931at2157; -.
DR PhylomeDB; Q8TN86; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AAM05793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002487}.
FT DOMAIN 43..205
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 296 AA; 32202 MW; 9CADF8EBA4671581 CRC64;
MSKTAPKTYI TSGHSACPGC CDIFAAKFAL MGAGPNCIIV NPTGCLEVTS TPYPKSAWQV
PWIHSLFENG GAVASGVEAG LKALGKKDDI KVIAIAGDGA TMDIGIRSIS GAFERGHDFT
YICMDNEAYM NTGVQRSSGT PFDASTTTSP PGKFSFGNPL PKKNMPAIMA AHGSPYVATT
TIGFPRDMIR KVKKATEIMG PTYIHAHAPC TTGWGFDTSK TLEVARLAVE TCLWPLYEME
NGQITQARKI KNPRPVEEYL RAQKRFQHLF TMEGGEEEIK KIQAMADWNI EYYGLQ
//
