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Database: UniProt
Entry: A0A1Q5G1P1_9ACTN
LinkDB: A0A1Q5G1P1_9ACTN
Original site: A0A1Q5G1P1_9ACTN 
ID   A0A1Q5G1P1_9ACTN        Unreviewed;       432 AA.
AC   A0A1Q5G1P1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Aldolase {ECO:0000313|EMBL:OKJ26518.1};
GN   ORFNames=AMK22_31790 {ECO:0000313|EMBL:OKJ26518.1};
OS   Streptomyces sp. CB01580.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703933 {ECO:0000313|EMBL:OKJ26518.1, ECO:0000313|Proteomes:UP000186318};
RN   [1] {ECO:0000313|EMBL:OKJ26518.1, ECO:0000313|Proteomes:UP000186318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01580 {ECO:0000313|EMBL:OKJ26518.1,
RC   ECO:0000313|Proteomes:UP000186318};
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:OKJ26518.1}.
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DR   EMBL; LIXJ01000035; OKJ26518.1; -; Genomic_DNA.
DR   RefSeq; WP_073791039.1; NZ_LIXJ01000035.1.
DR   AlphaFoldDB; A0A1Q5G1P1; -.
DR   STRING; 1703933.AMK22_31790; -.
DR   OrthoDB; 9808769at2; -.
DR   Proteomes; UP000186318; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186318}.
SQ   SEQUENCE   432 AA;  45999 MW;  6849C9E582C33F1D CRC64;
     MGQQEQVATS LAGTVGEEIG ASLTAVDAEL ARRYPGDPGT RQPVHTVYVP GDTFTSGTIR
     SWGDRALKAL DEHAPDAASF ASVLGIPDEL ADPVHDRVRA KLEREPVEDL RIDFEDGYGS
     RPDAEEDETA ARAARLVAEA YANGTAAPYM GIRMKCMEAA VRDRGIRTTD IFLTGLMRAG
     GLPDGLVLTL PKVTYPEQVT AFVRLLEAFE QTQGLPAGRI GFEIQIETSQ SILAADGTAA
     VARMIDAARG RATGLHYGTF DYSACVGVSA AYQASDHPAA DHAKAVMQVA AAGTGVRVCD
     GSTNVLPVGP THRVHEAWRL HHGLTRRALT RAYYQGWDMH PGHLPTRYAA VYTFYREGLE
     QAAARLAAYA ARIGGDVMDE PATAKALGGY LLRGIDCGAL DAAEVVRLTG LTRADLDAFA
     APRRAGLTVT AP
//
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