ID A0A0A1DRA9_NOCSI Unreviewed; 361 AA.
AC A0A0A1DRA9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:GEB14863.1};
DE SubName: Full=CoA ester lyase {ECO:0000313|EMBL:KAB2812428.1};
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:AIY19063.1};
DE EC=4.1.3.24 {ECO:0000313|EMBL:AIY19063.1};
GN Name=citE_2 {ECO:0000313|EMBL:GEB14863.1};
GN ORFNames=F9L07_11695 {ECO:0000313|EMBL:KAB2812428.1}, KR76_23920
GN {ECO:0000313|EMBL:AIY19063.1}, NSI01_31780
GN {ECO:0000313|EMBL:GEB14863.1};
OS Nocardioides simplex (Arthrobacter simplex).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Pimelobacter.
OX NCBI_TaxID=2045 {ECO:0000313|EMBL:AIY19063.1, ECO:0000313|Proteomes:UP000030300};
RN [1] {ECO:0000313|EMBL:AIY19063.1, ECO:0000313|Proteomes:UP000030300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2033D {ECO:0000313|EMBL:AIY19063.1,
RC ECO:0000313|Proteomes:UP000030300};
RX PubMed=25573942;
RA Shtratnikova V.Y., Schelkunov M.I., Pekov Y.A., Fokina V.V.,
RA Logacheva M.D., Sokolov S.L., Bragin E.Y., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Steroid-Transforming Nocardioides simplex VKM
RT Ac-2033D.";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0000313|EMBL:GEB14863.1, ECO:0000313|Proteomes:UP000318936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12069 {ECO:0000313|EMBL:GEB14863.1,
RC ECO:0000313|Proteomes:UP000318936};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Pimelobacter simplex NBRC 12069.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAB2812428.1, ECO:0000313|Proteomes:UP000449906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pch-N {ECO:0000313|EMBL:KAB2812428.1,
RC ECO:0000313|Proteomes:UP000449906};
RA Jeong S.E.;
RT "Pimelobacter sp. isolated from Paulinella.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009896; AIY19063.1; -; Genomic_DNA.
DR EMBL; BJMC01000015; GEB14863.1; -; Genomic_DNA.
DR EMBL; WBVM01000001; KAB2812428.1; -; Genomic_DNA.
DR RefSeq; WP_038681925.1; NZ_WBVM01000001.1.
DR AlphaFoldDB; A0A0A1DRA9; -.
DR STRING; 2045.KR76_23920; -.
DR KEGG; psim:KR76_23920; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_11; -.
DR OrthoDB; 5172636at2; -.
DR Proteomes; UP000030300; Chromosome.
DR Proteomes; UP000318936; Unassembled WGS sequence.
DR Proteomes; UP000449906; Unassembled WGS sequence.
DR GO; GO:0043959; F:L-erythro-3-methylmalyl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0050083; F:malyl-CoA 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:AIY19063.1};
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:UP000030300}.
FT DOMAIN 33..196
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 361 AA; 39031 MW; 00334D7F1B2B48CF CRC64;
MSHKSAKDFF RPLAVGAPLP LREIPARPSR AIHFFDPSNE KMAAKIPGMI GTVDVLLGNL
EDAVKADNKV AAREGLVKIA QATDFGPTQL WTRINALDSP WVLDDLTTLV PAIGEKLDVI
MVPKVQGAED IHYVDRLLAQ LEAKAGITKP ILIHAILETA RGVANVEEIC GASPRMQGLS
LGPADLAADR KMKTTRVGGG HPGYLVRQDP PRDAEGNSQI DAQRAIFQQD LWHYTIAKMV
DACATHGIYP YYGPFGDIAD VVACEDQFRN AFLLGCVGTW SLHPKQIAIA NRVFSPSVED
IAHARRVVAA MGDGTGAVMI DGKMEDDASL KQCLVLVALA EQLAEIDPEL KKTYDAIEVT
A
//
