ID A0A024H715_9MICC Unreviewed; 283 AA.
AC A0A024H715;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Fructose-bisphosphate aldolase class-II family protein {ECO:0000313|EMBL:CCQ47798.1};
GN Name=gatY {ECO:0000313|EMBL:CCQ47798.1};
GN ORFNames=ARTSIC4J27_3794 {ECO:0000313|EMBL:CCQ47798.1};
OS Pseudarthrobacter siccitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ47798.1, ECO:0000313|Proteomes:UP000035722};
RN [1] {ECO:0000313|Proteomes:UP000035722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT Producing Desiccation-Tolerant Microorganism.";
RL Genome Announc. Announc.2:e00526-e00514(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3};
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:CCQ47798.1}.
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DR EMBL; CAQI01000053; CCQ47798.1; -; Genomic_DNA.
DR RefSeq; WP_050056619.1; NZ_CAQI01000053.1.
DR AlphaFoldDB; A0A024H715; -.
DR STRING; 861266.ARTSIC4J27_3794; -.
DR OrthoDB; 9803995at2; -.
DR Proteomes; UP000035722; Unassembled WGS sequence.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR PANTHER; PTHR43060; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-LIKE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43060:SF17; L-THREONATE DEHYDROGENASE; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 81
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 183
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 211..213
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 232..235
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 283 AA; 29280 MW; 17350C7C888C8762 CRC64;
MRTRLDHLVT SALQHGSAVP AFTCYDFTTA LAVVAAAEES GRGVILLVAP KTAATPNGLR
LIGALRGLAD AAAVPVAVQL DHATDLSVMA DAVTAGADSV LADGSSLPYE DNIALVRAAR
DLLGPDVVLE AELGGLAGDE DRAFGADQSG VSVAGLTDSA QVEDFVSRTG AELLAVAVGN
VHGKYKGEPQ LRWDVLQDIA VRTHIPLVLH GASGIPAEEL VKAASMNVGK VNFNTELRTG
VLATLQAQLP AHRSDGENLQ GLLSHWNQAA RSFASTTLAT LTR
//
