ID A3CW20_METMJ Unreviewed; 582 AA.
AC A3CW20;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:ABN57570.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:ABN57570.1};
GN OrderedLocusNames=Memar_1643 {ECO:0000313|EMBL:ABN57570.1};
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407 {ECO:0000313|EMBL:ABN57570.1, ECO:0000313|Proteomes:UP000002146};
RN [1] {ECO:0000313|EMBL:ABN57570.1, ECO:0000313|Proteomes:UP000002146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1
RC {ECO:0000313|Proteomes:UP000002146};
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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DR EMBL; CP000562; ABN57570.1; -; Genomic_DNA.
DR RefSeq; WP_011844481.1; NC_009051.1.
DR AlphaFoldDB; A3CW20; -.
DR STRING; 368407.Memar_1643; -.
DR GeneID; 76729713; -.
DR KEGG; mem:Memar_1643; -.
DR eggNOG; arCOG02095; Archaea.
DR HOGENOM; CLU_000395_4_2_2; -.
DR OMA; GYHALEM; -.
DR OrthoDB; 6555at2157; -.
DR Proteomes; UP000002146; Chromosome.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005776; OadA.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01108; oadA; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000313|EMBL:ABN57570.1};
KW Pyruvate {ECO:0000313|EMBL:ABN57570.1}.
FT DOMAIN 9..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 502..582
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 582 AA; 63500 MW; 5798A90BF3598F71 CRC64;
MCAAKLDSLN ITDTTLRDAH QSLIATRLRT EDMLPLARAI DDVGFFSVEA WGGATFDSCI
RFLNDDPWER LRVLKAELRR TPIQMLLRGQ NLVGYRHYPD DVVEKFVEAS ARNGVDIFRV
FDALNDIRNM KKAMEEVKNV GAHLQGAISY TTSPVHSVAT FVEMAEELYT LGCDSICIKD
MAGLIMPHDA RDLITGIKKT ADVRVCLHSH CTSGVAPLSY QAAIDAGVDI LDTAMSPFAL
GTSQPPTESV VASVAGTARD TGIDLLPLRK VRNICRDMRG KYEPLFNSIA DRVDSDVLIY
QLPGGMISNL VSQLKEQDAL DRLDEVLREI PRVREDLGYP PLVTPTSQIV GTQAVFNVLM
DGERYRNVTK EVKDYVRGLY GRSPAPISPE IRRTIIGDEE PVTVRPADLL EPIYEQMKKE
AEEQGLVTRD EDVLTYILYP SVAPSFLRGE RQPEAIPEKA AAGPAGVAEI PRSMEVEVDG
EIFSVRIVTV EGGSVAAASA AAASAGAPRG DVAGGVKSNM QGMVLKVMAQ RGSTVRKGDT
LIVLEAMKME NPIPSPRDGT VSEIFVDAGD VVQNGDVLMV IE
//