ID S7TYD3_DESML Unreviewed; 686 AA.
AC S7TYD3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Carboxylase region-containing protein {ECO:0000313|EMBL:EPR42166.1};
GN ORFNames=dsmv_1683 {ECO:0000313|EMBL:EPR42166.1};
OS Desulfococcus multivorans DSM 2059.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfococcaceae; Desulfococcus.
OX NCBI_TaxID=1121405 {ECO:0000313|EMBL:EPR42166.1, ECO:0000313|Proteomes:UP000014977};
RN [1] {ECO:0000313|EMBL:EPR42166.1, ECO:0000313|Proteomes:UP000014977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2059 {ECO:0000313|EMBL:EPR42166.1,
RC ECO:0000313|Proteomes:UP000014977};
RX PubMed=23950126;
RA Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT "Draft genome sequences for three mercury-methylating, sulfate-reducing
RT bacteria.";
RL Genome Announc. 1:e00618-e00613(2013).
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:EPR42166.1}.
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DR EMBL; ATHJ01000068; EPR42166.1; -; Genomic_DNA.
DR RefSeq; WP_020876067.1; NZ_FUWN01000014.1.
DR AlphaFoldDB; S7TYD3; -.
DR STRING; 897.B2D07_17075; -.
DR PATRIC; fig|1121405.3.peg.1131; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000014977; Unassembled WGS sequence.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
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 Reference proteome {ECO:0000313|Proteomes:UP000014977}.
FT DOMAIN 23..289
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 609..686
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 562..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 74896 MW; B75CE1EBD6447DE2 CRC64;
MSDQVKMTEM NYSPDRPKAE NPIKIMDLSL RDGHQSLFAT RGRTEDMIPV AELMDEVGFW
AVETWGGATF DTMHRFLNED PWQRLRTLKR YFKKTPFSML LRAQNLVGYR NYADDLAEAF
VERTAENGMD IFRTFDALND YRNFETVVKG IKKAGKHFQG CICYTMTEPR LGGEIYNLDY
YVNKAKDLEA MGADSICIKD MAGLIAPYDA YNLIKALKAA VKPPIHLHSH FTSGMSPMSH
LKAIEAGVDI IDTCMTPYAY RTSHAAVEPL VMALLGTNRD TGFDIKKLAR INEILEKEVM
PKYKHLLDDS KVSVIDINVL LHQTPGGMLS NLVNQLREMD ALDKIDQVYK ELPRVRKELG
AIPLVTPTSQ IVGIQTVNNV LFDDENERYK MITAQVKDLC YGLYGKTAIP IDPEVQKKAL
KGYSRGEEPI TCRPAEVLEP ELEKAREEIG DLAKDIDDVI LYAIYPVTGR KFLKWKYGVE
APPKEVLPRT IEDVKKDEEL IKKAKAGLLV EKAPAKDVPE KGEATRKFNV FVDGDYFAVE
VDEPGGAPII AYQAPAQAAP ATPAAPAAPA APTAPGRPAP AAPAPPVKPT PAAPAAPKAA
APAPAPAAPA PAADASGTPL TAPMPGMIVS YAKKVGDAVK KGDTVVILEA MKMENALPAP
CDGTVKAVNF SSGDSVAKGA VLCVIG
//
