ID D1A979_THECD Unreviewed; 313 AA.
AC D1A979;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:ACY96775.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:ACY96775.1};
GN OrderedLocusNames=Tcur_1192 {ECO:0000313|EMBL:ACY96775.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY96775.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY96775.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001738; ACY96775.1; -; Genomic_DNA.
DR RefSeq; WP_012851559.1; NC_013510.1.
DR AlphaFoldDB; D1A979; -.
DR STRING; 471852.Tcur_1192; -.
DR KEGG; tcu:Tcur_1192; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_11; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR32308:SF10; CITRATE LYASE SUBUNIT BETA; 1.
DR PANTHER; PTHR32308; LYASE BETA SUBUNIT, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G13030)-RELATED; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ACY96775.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918}.
FT DOMAIN 5..236
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 313 AA; 34706 MW; B244E12AE174172F CRC64;
MRSRRSTLAV PGSNPRFIEK AQGLPADEIF LDLEDAVAPS AKEEARKNVV AALNEGDWDG
KIRVVRINDL RTHWAYRDVI EVVEGAGAKL DCLMLPKVQE PDDVRWLDRL LTQIETAMGY
PVGRIGIEAQ IEDARGMTNI DAIAASSPRL ETLIFGPGDF MASINMKTLV VGEQPPGYTE
GDAYHYILMR ILLAARAHDL QAIDGPYFNV RDVESFKRVA RRSAALGFDG KWVLHPSQIE
AANEVFSPTQ EDYDHAELIL DAYEYYTTVE GRGAAMLGDE MIDEASRKMA LVIAAKGRAA
GLRRTKFFQP PAD
//