ID Q9WZH5_THEMA Unreviewed; 515 AA.
AC Q9WZH5; G4FDA8;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE SubName: Full=Propionyl-CoA carboxylase, beta subunit {ECO:0000313|EMBL:AAD35798.1};
GN OrderedLocusNames=TM_0716 {ECO:0000313|EMBL:AAD35798.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274 {ECO:0000313|EMBL:AAD35798.1, ECO:0000313|Proteomes:UP000008183};
RN [1] {ECO:0000313|EMBL:AAD35798.1, ECO:0000313|Proteomes:UP000008183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000313|Proteomes:UP000008183};
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., Heidelberg J.,
RA Sutton G.G., Fleischmann R.D., White O., Salzberg S.L., Smith H.O.,
RA Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0007829|PDB:1VRG}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MG(2+).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of propionyl-CoA carboxylase, beta subunit (TM0716) from
RT THERMOTOGA MARITIMA at 2.30 A resolution.";
RL Submitted (FEB-2005) to the PDB data bank.
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DR EMBL; AE000512; AAD35798.1; -; Genomic_DNA.
DR PIR; C72344; C72344.
DR RefSeq; NP_228525.1; NC_000853.1.
DR RefSeq; WP_004081020.1; NZ_CP011107.1.
DR PDB; 1VRG; X-ray; 2.30 A; A/B/C/D/E/F=1-515.
DR PDBsum; 1VRG; -.
DR AlphaFoldDB; Q9WZH5; -.
DR SMR; Q9WZH5; -.
DR PaxDb; 243274-THEMA_01085; -.
DR EnsemblBacteria; AAD35798; AAD35798; TM_0716.
DR KEGG; tma:TM0716; -.
DR KEGG; tmw:THMA_0731; -.
DR PATRIC; fig|243274.17.peg.717; -.
DR InParanoid; Q9WZH5; -.
DR OrthoDB; 9803706at2; -.
DR EvolutionaryTrace; Q9WZH5; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IBA:GO_Central.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1VRG}; Metal-binding {ECO:0007829|PDB:1VRG};
KW Reference proteome {ECO:0000313|Proteomes:UP000008183}.
FT DOMAIN 3..259
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 263..497
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:1VRG"
FT BINDING 379
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:1VRG"
SQ SEQUENCE 515 AA; 56415 MW; 1A3FF6445F16BA7D CRC64;
MSLRDKIEEL KKIEKEIEQG GGPEKVEKQH RAGKLTAWER LELLLDPGTF VEIDKFVEHR
NTYFGLDKVK LPRDGVITGV GEINGRKVAV FSQDFTVMGG SLGEMHAKKI VKLLDLALKM
GIPVIGINDS GGARIQEGVD ALAGYGEIFL RNTLASGVVP QITVIAGPCA GGAVYSPALT
DFIVMVDQTA RMFITGPNVI KAVTGEEISQ EDLGGAMVHN QKSGNAHFLA DNDEKAMSLV
RTLLSYLPSN NAEEPPVEDP DTSLETPEDI LDILPDNPNK GYDVRDVIKR VVDHGEFFEV
QPYFAKNIVI GFARIQGKTV GIVANQPSVL AGVLDIDSSD KAARFIRFLD AFNIPILTFV
DTPGYLPGVA QEHGGIIRHG AKLLYAYSEA TVPKITVILR KAYGGAYIAM GSKHLGADMV
LAWPSAEIAV MGPEGAANII FKREIEASSN PEETRRKLIE EYKQQFANPY IAASRGYVDM
VIDPRETRKY IMRALEVCET KVEYRPKKKH GNIPL
//
