ID C1DL12_AZOVD Unreviewed; 531 AA.
AC C1DL12;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446};
DE AltName: Full=Isocitrase {ECO:0000256|ARBA:ARBA00031022};
DE AltName: Full=Isocitratase {ECO:0000256|ARBA:ARBA00031921};
GN OrderedLocusNames=Avin_28420 {ECO:0000313|EMBL:ACO79014.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO79014.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO79014.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023531};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
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DR EMBL; CP001157; ACO79014.1; -; Genomic_DNA.
DR RefSeq; WP_012701401.1; NC_012560.1.
DR AlphaFoldDB; C1DL12; -.
DR STRING; 322710.Avin_28420; -.
DR EnsemblBacteria; ACO79014; ACO79014; Avin_28420.
DR KEGG; avn:Avin_28420; -.
DR eggNOG; COG2224; Bacteria.
DR HOGENOM; CLU_038243_0_0_6; -.
DR OrthoDB; 8629576at2; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ACO79014.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 531 AA; 59102 MW; 755D15BFF0995417 CRC64;
MSAYQNEIKA LAALKEKNGS AWSAINPEYA ARMRIQNRFK TGLDVAKYTA AIMRKDMAEY
DADSSVYTQS LGCWHGFIGQ QKLISIKKHL KTTDKKYLYL SGWMVAALRS DFGPLPDQSM
HEKTAVSSLI EELYTFLRQA DARELDLLFS ALDDARNAGD KAKEQEILKQ IDGFETHVVP
IIADIDAGFG NAEATYLLAR KMIEAGACCI QIENQVSDEK QCGHQDGKVT VPHEDFLAKI
NAVRYAFLEL GVDDGVIVAR TDSLGAGLTK QIAVTRQEGD LGDKYNAFLD CEEISPAEMK
NGDVVLNRNG KLLRPKRLAS GLFQFRKGTG EDRCVLDCIT SLQNGADLLW IETEKPHIGQ
IKGMVDRIRE AIPNAKLVYN NSPSFNWTLN FRQQVFDTWA AEGKDVAKYD RAKLMSVEYD
ETELALEADA RIRTFQRDAA AQAGIFHHLI TLPTYHTAAL STDNLAKGYF AEEGMLAYVK
GVQRQEIRQS IACVKHQNMA GSDIGDNHKE YFAGEAALKA GGKDNTMNQF H
//
