ID K9HP28_9PROT Unreviewed; 327 AA.
AC K9HP28;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Malyl-CoA lyase {ECO:0000313|EMBL:EKV32053.1};
GN ORFNames=C882_3117 {ECO:0000313|EMBL:EKV32053.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV32053.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV32053.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV32053.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(2013).
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:EKV32053.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANHY01000004; EKV32053.1; -; Genomic_DNA.
DR RefSeq; WP_009539314.1; NZ_ANHY01000004.1.
DR AlphaFoldDB; K9HP28; -.
DR STRING; 1238182.C882_3117; -.
DR PATRIC; fig|1238182.3.peg.865; -.
DR eggNOG; COG2301; Bacteria.
DR OrthoDB; 9800547at2; -.
DR Proteomes; UP000009881; 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:EKV32053.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009881}.
FT DOMAIN 20..259
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 327 AA; 35203 MW; 3C1179A93681351F CRC64;
MSFTVAEPAP PRLNRSEQAV PGSNTRFLEK AAAGDADMVF LDLEDAVAPS EKAQARKNII
EAVNDLDWGG KTISVRINGL DTHYMYQDVI QIMENAVDKI DLIMIPKAGT ASDIYAVDML
CTQIEQAKGW TKKVGFEMII ETALGMQNVH EIAAASKRNE SLHFGVADYA ASTAARTVGI
GGPNPNYGVL TDADEAGNRD FHWGDMWHYA IARMVVAARA NGLRPIDGPF GDFSDAEGYK
AQARRAAILG CEGKWAIHPN QVALANEIYS PSDKDVAQAQ AILDAMEEAQ KSGQGAVTLN
GKLIDIASIK QAQVLVKMAE QIKAAGK
//