ID C4IUY5_BRUAO Unreviewed; 334 AA.
AC C4IUY5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Citrate lyase subunit beta {ECO:0000313|EMBL:EEP61878.1};
GN ORFNames=BAAA_7000362 {ECO:0000313|EMBL:EEP61878.1};
OS Brucella abortus str. 2308 A.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=641140 {ECO:0000313|EMBL:EEP61878.1, ECO:0000313|Proteomes:UP000003313};
RN [1] {ECO:0000313|EMBL:EEP61878.1, ECO:0000313|Proteomes:UP000003313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 A {ECO:0000313|EMBL:EEP61878.1,
RC ECO:0000313|Proteomes:UP000003313};
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.;
RL Submitted (MAY-2009) 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}.
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:EEP61878.1}.
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DR EMBL; ACOR01000007; EEP61878.1; -; Genomic_DNA.
DR AlphaFoldDB; C4IUY5; -.
DR Proteomes; UP000003313; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:EEP61878.1};
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 52..270
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 171
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 334 AA; 35775 MW; B9A216A85DBBFDE2 CRC64;
MVLMALNKMS VVLPPVSFQT ISGLGPQLFS VLALWGCSVH KSGMKTIVRP RRSVLFVPAA
NTRALEKSLT LSADCVIYDL EDSVAPEAKA AACEALAAHL SAHPKVAFER IVRVNAADTP
WGRDDVAAVA KMAVNAVLLP KVERPQDVIE AANHLDRQDA DPAMGVWAMI ETPRGILNVD
EIAVLGHRSA VRLACFVVGP NDIARETGLR SQPGRPYLAP WLMQIVLAAR AGGIAVLDGV
YNDFRDSAGF EAECAQGAAM GFDGKTLIHP GQIEAANRAF SPTEEEVAHA RAVREIFARP
ENAGKGVVSL DGQMVERLHL EMAERILAKA GINL
//
