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Database: UniProt
Entry: M0II76_9EURY
LinkDB: M0II76_9EURY
Original site: M0II76_9EURY 
ID   M0II76_9EURY            Unreviewed;       433 AA.
AC   M0II76;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Malate synthase {ECO:0000313|EMBL:ELZ96476.1};
GN   ORFNames=C440_04993 {ECO:0000313|EMBL:ELZ96476.1};
OS   Haloferax mucosum ATCC BAA-1512.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=662479 {ECO:0000313|EMBL:ELZ96476.1, ECO:0000313|Proteomes:UP000011550};
RN   [1] {ECO:0000313|EMBL:ELZ96476.1, ECO:0000313|Proteomes:UP000011550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1512 {ECO:0000313|EMBL:ELZ96476.1,
RC   ECO:0000313|Proteomes:UP000011550};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ96476.1}.
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DR   EMBL; AOLN01000007; ELZ96476.1; -; Genomic_DNA.
DR   RefSeq; WP_008318830.1; NZ_AOLN01000007.1.
DR   AlphaFoldDB; M0II76; -.
DR   STRING; 662479.C440_04993; -.
DR   PATRIC; fig|662479.7.peg.1022; -.
DR   OrthoDB; 9170at2157; -.
DR   Proteomes; UP000011550; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 1.20.58.1560; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; NF041315; malate_syn_AceB_Halo; 1.
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   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          40..253
FT                   /note="HpcH/HpaI aldolase/citrate lyase"
FT                   /evidence="ECO:0000259|Pfam:PF03328"
SQ   SEQUENCE   433 AA;  48398 MW;  8B979CD6321984E6 CRC64;
     MTERRHDREF VRTFFTSPTA VEGEADSAKM LRRAAQLRGM QAPDVWVPDN EDATAPSMRD
     EGAENIVEVV VEHGADFPGE IHPRMVWHRD SPTTRYQGFQ HMLEIADPER GAIEHIDGFV
     IPEVGDIDDW KKADEFFTIV ENEHDLEEGS LKMSVIIESG QAELAMGTLR EEMGKPTNNL
     ERLFLLVDGE VDYTKDMRAM TPTGELPEWP ELRHNTSRGA SAAGLIAVDG PYDDIRNVEG
     YHERMAENRA KGMLGIWSLT PGQVVEANTS PLPPKTGSWL LDIDGEQVEL EAEDGAEVYD
     GDHLSLEATD GGYQLHIDGT TRTLDADELR EELHGMTSYV PSMDDIVDSM EEFEAAKEAG
     RGAIAMEQSA TLRIGGTEID ISKDRMWDEA TYQAAMTPIN LFQDVYENRP DQHEELNERY
     GADVVSRAME VGL
//
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