ID A0A0B4XWF2_9PROT Unreviewed; 328 AA.
AC A0A0B4XWF2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:AJD50662.1};
GN ORFNames=TH3_02680 {ECO:0000313|EMBL:AJD50662.1};
OS Thalassospira xiamenensis M-5 = DSM 17429.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1123366 {ECO:0000313|EMBL:AJD50662.1, ECO:0000313|Proteomes:UP000007127};
RN [1] {ECO:0000313|EMBL:AJD50662.1, ECO:0000313|Proteomes:UP000007127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M-5 {ECO:0000313|EMBL:AJD50662.1,
RC ECO:0000313|Proteomes:UP000007127};
RX PubMed=23209216; DOI=10.1128/JB.01904-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of Thalassospira xiamenensis type strain M-5.";
RL J. Bacteriol. 194:6957-6957(2012).
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; CP004388; AJD50662.1; -; Genomic_DNA.
DR RefSeq; WP_007088928.1; NZ_FTON01000002.1.
DR AlphaFoldDB; A0A0B4XWF2; -.
DR STRING; 1123366.TH3_02680; -.
DR GeneID; 31926239; -.
DR KEGG; txi:TH3_02680; -.
DR eggNOG; COG2301; Bacteria.
DR HOGENOM; CLU_044864_0_1_5; -.
DR Proteomes; UP000007127; Chromosome.
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:AJD50662.1};
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 17..259
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 76
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"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 328 AA; 35460 MW; 156593B0E5A9519D CRC64;
MSFTTPTPAP ARLNRSELAV PGSRIELFEK AARSKADAIF LDLEDAVAPN DKEQARKNII
AAINDIDWGD KVLSVRINGL DTHYMYRDVV DVLEQAGDRL DLIMIPKVGT AADVYALDMM
ATQIEAAKGR KKRIGFELII ETALGMQNIH EIAGASKRNE SLHFGVADYA ASTKAMTTGI
GGPNPHYGVL TDKDGDNPRD YHWGDMWHYA IARMVVAARA NGLRPIDGPF GDFSDPDGYR
AQAARAMVLG CEGKWAIHPS QITLANDVYS PSEAEVTKAK RILEAMTKAQ AEGAGAVALD
GRLIDIASIK QAEVMVKQAE AIAARDAG
//
