ID A9MDS6_BRUC2 Unreviewed; 274 AA.
AC A9MDS6;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=HpcH/HpaI aldolase {ECO:0000313|EMBL:ABX63364.1};
GN OrderedLocusNames=BCAN_B0168 {ECO:0000313|EMBL:ABX63364.1};
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179 {ECO:0000313|EMBL:ABX63364.1, ECO:0000313|Proteomes:UP000001385};
RN [1] {ECO:0000313|EMBL:ABX63364.1, ECO:0000313|Proteomes:UP000001385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854 {ECO:0000313|Proteomes:UP000001385};
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC {ECO:0000256|ARBA:ARBA00005568}.
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DR EMBL; CP000873; ABX63364.1; -; Genomic_DNA.
DR RefSeq; WP_002966416.1; NC_010104.1.
DR AlphaFoldDB; A9MDS6; -.
DR GeneID; 58777884; -.
DR KEGG; bcs:BCAN_B0168; -.
DR HOGENOM; CLU_044864_2_0_5; -.
DR PhylomeDB; A9MDS6; -.
DR Proteomes; UP000001385; Chromosome II.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
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 Pfam; PF03328; HpcH_HpaI; 1.
DR PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2}.
FT DOMAIN 9..208
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 274 AA; 29008 MW; 2D13C2E692AFF709 CRC64;
MVSIASIRAP LFVPADRPDR FSKAAASGTD CVILDLEDAV APKAKDAARA ALDTSFTDLP
VMVRINPHGT PWHEADMAAV ARLDVAGVIL PKAETAERIE AAARMLDLPL IALVETARGL
ANARSIAAAS GVVRLAFGSI DFCADLACAH MREILLPARV ELVMASRLAG IAAPIDGVTP
GFNDPVMCHQ DAAHARALGM MGKLCIHPRQ ISEVLRAFAW SDQEIDWARR VLASGEGAIS
IDGMMVDEPV RIRARTILEQ ADIGAAPVLT KPTG
//
