ID A0A0Q9NC10_9MICC Unreviewed; 253 AA.
AC A0A0Q9NC10;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Aldolase {ECO:0000313|EMBL:KRE71731.1};
GN ORFNames=ASG77_12010 {ECO:0000313|EMBL:KRE71731.1};
OS Arthrobacter sp. Soil762.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE71731.1, ECO:0000313|Proteomes:UP000051715};
RN [1] {ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE71731.1, ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|EMBL:KRE71731.1,
RC ECO:0000313|Proteomes:UP000051715};
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 -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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:KRE71731.1}.
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DR EMBL; LMSG01000019; KRE71731.1; -; Genomic_DNA.
DR RefSeq; WP_056347099.1; NZ_LMSG01000019.1.
DR AlphaFoldDB; A0A0Q9NC10; -.
DR OrthoDB; 3353438at2; -.
DR Proteomes; UP000051715; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR30502; 2-KETO-3-DEOXY-L-RHAMNONATE ALDOLASE; 1.
DR PANTHER; PTHR30502:SF0; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 18..239
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 253 AA; 26171 MW; D006E0BDCA808E62 CRC64;
MTAASFAAKA RANEPVVGYW VVLDSPVSTE RVARLGYDYV ALDAQHGLMG YSGWLHGLMA
IDAAGAAGIV RVPSNNAAFI GQALDAGAAG VIVPLVNNAE EAAAAVRAVR YPPHGMRSYG
PMRSALRIGP VPAETDATVL CLAMIETPEG LENVKEICAV PGIDGVYIGP SDLCLAVGGK
FPNDPDVAEE FNAALVTIRE AAQAAGVIAA IHTASGEIAR QRIAEGFTFV TVASDLTHLE
IAAANHLSRA RGE
//