ID A0A1Q5MW38_9ACTN Unreviewed; 297 AA.
AC A0A1Q5MW38;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:OKK18419.1};
GN ORFNames=AMK16_19125 {ECO:0000313|EMBL:OKK18419.1};
OS Streptomyces sp. CB00455.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK18419.1, ECO:0000313|Proteomes:UP000185643};
RN [1] {ECO:0000313|EMBL:OKK18419.1, ECO:0000313|Proteomes:UP000185643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00455 {ECO:0000313|EMBL:OKK18419.1,
RC ECO:0000313|Proteomes:UP000185643};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK18419.1}.
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DR EMBL; LIVQ01000004; OKK18419.1; -; Genomic_DNA.
DR RefSeq; WP_073917346.1; NZ_LIVQ01000004.1.
DR AlphaFoldDB; A0A1Q5MW38; -.
DR STRING; 1703927.AMK16_19125; -.
DR OrthoDB; 5172636at2; -.
DR Proteomes; UP000185643; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000185643}.
FT DOMAIN 10..218
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 297 AA; 30790 MW; CD8823BD563C1281 CRC64;
MTGTARAVPR SILYTPALSL DRVVKAWSYD ADVHLIDLED AVPPGGKAAA RLVCRAALEK
APRPADLAVR VNGLGTVEAV HDLVMLTASP VRPGFVVMTM VRSAVEVTLL RDTLASAGAH
PEIYVTVETV EAVTGMDAIA AAADGLVLGS ADLAATLGIE IGWAGLLAAR QAMALAAARH
GAGCIDTANF RLAEPQVLAE EIGRARELGF HGKATVHPAE LGAINAALRP CPDDLRQARR
VTEAVRAADG GVAVLDGSMV GPPFARLARD TVARGDAWAG RFGPERGQGG EVGRDDH
//
