ID D2RZC2_HALTV Unreviewed; 288 AA.
AC D2RZC2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Citrate (Pro-3S)-lyase {ECO:0000313|EMBL:ADB60046.1};
DE EC=4.1.3.6 {ECO:0000313|EMBL:ADB60046.1};
GN OrderedLocusNames=Htur_1154 {ECO:0000313|EMBL:ADB60046.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB60046.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB60046.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; CP001860; ADB60046.1; -; Genomic_DNA.
DR RefSeq; WP_012942352.1; NC_013743.1.
DR AlphaFoldDB; D2RZC2; -.
DR STRING; 543526.Htur_1154; -.
DR GeneID; 8741743; -.
DR KEGG; htu:Htur_1154; -.
DR eggNOG; arCOG00760; Archaea.
DR HOGENOM; CLU_044864_2_1_2; -.
DR OrthoDB; 9170at2157; -.
DR Proteomes; UP000001903; Chromosome.
DR GO; GO:0016829; F:lyase activity; 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:SF0; HPCH_HPAI DOMAIN-CONTAINING PROTEIN; 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:ADB60046.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842}.
FT DOMAIN 4..222
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 288 AA; 31103 MW; CF21DBCF83D195C6 CRC64;
MVRRSVLFTP GDRPEMLRKA PAAGADVIVF DLEDAVAPQR KVEARESVRE VLTDLAFDPD
CEVCVRVNAG DSALAADLET VLEPAESDAD RRLDSVMAPK VASAADVRDL EDEIAKYDCT
LPVFALIESA AGVLAAPEIA AARATDALVF GAEDLSADIG ATRSAEGTEV LYARERVVIA
AAAHDCTAID TLVTDFEDER RLREDADRSV RLGYDGKLAI HPAQVDPINE AFTPDEADRK
WAERVLEAKR EADAEGRGVF EVDGEMIDAP LIAQAKRIQE RAAADDEN
//
