ID D1B796_THEAS Unreviewed; 347 AA.
AC D1B796;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Citrate lyase ligase {ECO:0000313|EMBL:ACZ19887.1};
DE EC=6.2.1.22 {ECO:0000313|EMBL:ACZ19887.1};
GN OrderedLocusNames=Taci_1673 {ECO:0000313|EMBL:ACZ19887.1};
OS Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS (Selenomonas acidaminovorans).
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Thermanaerovibrio.
OX NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19887.1, ECO:0000313|Proteomes:UP000002030};
RN [1] {ECO:0000313|EMBL:ACZ19887.1, ECO:0000313|Proteomes:UP000002030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49978 / DSM 6589 / Su883
RC {ECO:0000313|Proteomes:UP000002030};
RX PubMed=21304665; DOI=10.4056/sigs.40645;
RA Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT (Su883).";
RL Stand. Genomic Sci. 1:254-261(2009).
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DR EMBL; CP001818; ACZ19887.1; -; Genomic_DNA.
DR RefSeq; WP_012870396.1; NC_013522.1.
DR RefSeq; YP_003318169.1; NC_013522.1.
DR AlphaFoldDB; D1B796; -.
DR STRING; 525903.Taci_1673; -.
DR EnsemblBacteria; ACZ19887; ACZ19887; Taci_1673.
DR KEGG; tai:Taci_1673; -.
DR PATRIC; fig|525903.6.peg.1663; -.
DR eggNOG; COG3053; Bacteria.
DR HOGENOM; CLU_063190_0_0_0; -.
DR OrthoDB; 9779753at2; -.
DR Proteomes; UP000002030; Chromosome.
DR GO; GO:0008771; F:[citrate (pro-3S)-lyase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR005216; Citrate_lyase_ligase.
DR InterPro; IPR013166; Citrate_lyase_ligase_C.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00124; cit_ly_ligase; 1.
DR PANTHER; PTHR40599; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR PANTHER; PTHR40599:SF1; [CITRATE [PRO-3S]-LYASE] LIGASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF08218; Citrate_ly_lig; 1.
DR SMART; SM00764; Citrate_ly_lig; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ACZ19887.1}; Lyase {ECO:0000313|EMBL:ACZ19887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002030}.
FT DOMAIN 1..127
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 347 AA; 38662 MW; C0C38673FDEFB744 CRC64;
MSFGVETEFL DPASGVPEEV LSLLYAEGLR FEGADVTVLL RMNRRPAATA SLDGQVIKMV
AVDPEYRSMG LSAQAVSRLL EWARPRGMGH FFVYTKPSEA DKFESLGFCQ IGSSPGAVLL
EMGRPNAEDF RRGLEELRLR VGVEESSAIV MNANPFTRGH RYLAERASSA SEHLFVVVVR
SDRSSFPFED RIRMVRLGLE DLGNVTVVDG GDYAVSSATF PTYFLRDPSM EEVIRIQTRL
DLDLFGRIFV PALRIRSRFV GTEPYCPVTG LYNQAMREVL PRFGVQVVEV PRLEEGGSAV
SASLVRRAMA EGDPRGLEAL LPPTSYRYIM DNWDRLRERV LSSKGGH
//
