ID A0A1E7KJW4_9ACTN Unreviewed; 325 AA.
AC A0A1E7KJW4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:OEV04215.1};
GN ORFNames=AN216_08410 {ECO:0000313|EMBL:OEV04215.1};
OS Streptomyces oceani.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEV04215.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEV04215.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEV04215.1,
RC ECO:0000313|Proteomes:UP000176101};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OEV04215.1}.
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DR EMBL; LJGU01000114; OEV04215.1; -; Genomic_DNA.
DR RefSeq; WP_070195962.1; NZ_LJGU01000114.1.
DR AlphaFoldDB; A0A1E7KJW4; -.
DR STRING; 1075402.AN216_08410; -.
DR PATRIC; fig|1075402.3.peg.4492; -.
DR OrthoDB; 9768429at2; -.
DR Proteomes; UP000176101; 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 4: Predicted;
KW Lyase {ECO:0000313|EMBL:OEV04215.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR015582-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR015582-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000176101}.
FT DOMAIN 16..246
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-1"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR015582-2"
SQ SEQUENCE 325 AA; 35417 MW; FA8DBC42C0106C0C CRC64;
MTAASAEPAG RLRPRRSCMA VPGSNPRFLE KAQGLPADQV FLDLEDACAP LAKEDARHSI
VKALNEGDWR GKTRVVRVND WTTHWTYRDV ITVVEGAGAN LDCLMLPKVQ DAAQVRALDM
LLGQIERTVG LEVGRIGIEA QIENARGLVN VDDIAAASPR LETIIFGPAD FMASINMKSL
VVGEQPPGYP ADAYHYILMR ILMAARANDL QAIDGPYLQI RNLDGYREVA QRAAALGFDG
KWVLHPGQVE ASNEIFSPSQ EDYDHAELIL DAYEHFTSEE GGRKGSAMIG DEMIDEASRK
MALVIAGKGR AAGMTRTSTF TPPEA
//
