ID A0A0Q5VUQ6_9ACTN Unreviewed; 408 AA.
AC A0A0Q5VUQ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:KQS60906.1};
GN ORFNames=ASG36_08700 {ECO:0000313|EMBL:KQS60906.1};
OS Geodermatophilus sp. Leaf369.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS60906.1, ECO:0000313|Proteomes:UP000051830};
RN [1] {ECO:0000313|EMBL:KQS60906.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60906.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS60906.1, ECO:0000313|Proteomes:UP000051830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf369 {ECO:0000313|EMBL:KQS60906.1,
RC ECO:0000313|Proteomes:UP000051830};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS60906.1}.
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; LMQA01000001; KQS60906.1; -; Genomic_DNA.
DR RefSeq; WP_055761979.1; NZ_LMQA01000001.1.
DR AlphaFoldDB; A0A0Q5VUQ6; -.
DR STRING; 1736354.ASG36_08700; -.
DR OrthoDB; 9808769at2; -.
DR Proteomes; UP000051830; 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:UP000051830}.
SQ SEQUENCE 408 AA; 42666 MW; AAD808FA90081618 CRC64;
MTPETAVSGV TEEVLAELDR RLGPVDDARA AAYPGERSTR QPVHTCYVPA DAVVPGLVAS
WGEQALAALD EHGLPDLGLE AGLVEQVLPR VREKLAREPV EDLRVDSEDG YRGPPDREDE
DVARAAQVLA AEAALPPFWG TRAKSLEGPT RRRGVRSLDL FLGGLAGTGR AIVTLPKVTA
VEQVAAFLPV LDALEQAHGL ALDLELQVET PQAVLGADGV ATLAAMLHAG GGRVTGLHYG
TYDYSASLGI AAAHQASDHP AADHAKATMQ VAVAGTGARA VDGSTNVLPV GARDAVHHGW
QLHAGLVRRA LERGFYQGWD LHPAQLVTRY VATYAFFRAA LPAAGARLAA YVSRVDGGVL
DEPATARALA SVVLRGLDCG ALDAAEVEAA TGLDRPVLDR LAGRARPG
//