ID G7GPA0_9ACTN Unreviewed; 317 AA.
AC G7GPA0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Putative lyase {ECO:0000313|EMBL:GAB05425.1};
GN ORFNames=GOAMR_34_00920 {ECO:0000313|EMBL:GAB05425.1};
OS Gordonia amarae NBRC 15530.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB05425.1, ECO:0000313|Proteomes:UP000006023};
RN [1] {ECO:0000313|EMBL:GAB05425.1, ECO:0000313|Proteomes:UP000006023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB05425.1,
RC ECO:0000313|Proteomes:UP000006023};
RA Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:GAB05425.1}.
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DR EMBL; BAED01000034; GAB05425.1; -; Genomic_DNA.
DR RefSeq; WP_005186479.1; NZ_BAED01000034.1.
DR AlphaFoldDB; G7GPA0; -.
DR STRING; 1075090.GOAMR_34_00920; -.
DR eggNOG; COG2301; Bacteria.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000006023; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:GAB05425.1};
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:UP000006023}.
FT DOMAIN 8..239
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 317 AA; 34256 MW; AB53BF18E0F94F74 CRC64;
MVSYRPRRST LAVPGSSQKF IDKARSLNPD ALFLDLEDAC APAAKADGRV NVVKALNEGG
FGDTTRVVRI NDWTTEWTYR DVVDVVSGAG ANLDCLMLPK VQSAAQVQAL DLLVTQIEKA
EGLEVGRIGF EIQIENAKGL LAVNEIAAAS PRNETLIFGP ADFMASIQMK SLVVGEQPDG
YDVGDAYHHI LMTLLMAARA HDLQVIDGPY LAIKDLDGLR RVAGRSAALG FDGKWALHPT
QVDIVNDIFS PRQADYDHAE NILDAYDWCT SVEGGARGAA MLGDEMIDEA SRKMALVISA
KGRAAGMSRT DVWTPPQ
//
