Legends: 1, ACT_SITE Proton acceptor. {ECO:0000255|HAMAP- Rule:MF_00641}; 2, ACT_SITE Proton donor. {ECO:0000255|HAMAP- Rule:MF_00641}; 3, Magnesium. {ECO:0000255|HAMAP- Rule:MF_00641}; 4, BINDING Acetyl-CoA; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_00641}; 5, BINDING Acetyl-CoA. {ECO:0000255|HAMAP- Rule:MF_00641}; 6, BINDING Glyoxylate. {ECO:0000255|HAMAP- Rule:MF_00641}; 7, Cysteine sulfenic acid (-SOH). {ECO:0000255|HAMAP-Rule:MF_00641}; 8, REGION Acetyl-CoA binding. {ECO:0000255|HAMAP- Rule:MF_00641}; 9, REGION Glyoxylate binding. {ECO:0000255|HAMAP- Rule:MF_00641}.
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ID MASZ_CHRSD Reviewed; 742 AA.
AC Q1QSR0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 30-NOV-2016, entry version 70.
DE RecName: Full=Malate synthase G {ECO:0000255|HAMAP-Rule:MF_00641};
DE EC=2.3.3.9 {ECO:0000255|HAMAP-Rule:MF_00641};
GN Name=glcB {ECO:0000255|HAMAP-Rule:MF_00641};
GN OrderedLocusNames=Csal_3154;
OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS 13768).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA Canovas D., Richardson P.;
RT "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC condensation and subsequent hydrolysis of acetyl-coenzyme A
CC (acetyl-CoA) and glyoxylate to form malate and CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + glyoxylate = (S)-malate +
CC CoA. {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00641};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate
CC from isocitrate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00641}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00641}.
DR EMBL; CP000285; ABE60498.1; -; Genomic_DNA.
DR RefSeq; WP_011508444.1; NC_007963.1.
DR ProteinModelPortal; Q1QSR0; -.
DR STRING; 290398.Csal_3154; -.
DR EnsemblBacteria; ABE60498; ABE60498; Csal_3154.
DR KEGG; csa:Csal_3154; -.
DR PATRIC; 21450192; VBIChrSal113723_3174.
DR eggNOG; ENOG4107QP3; Bacteria.
DR eggNOG; COG2225; LUCA.
DR HOGENOM; HOG000220740; -.
DR KO; K01638; -.
DR OMA; GYNEVRG; -.
DR OrthoDB; POG091H05P0; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000000239; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-HAMAP.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00728; malate_synt_G; 1.
DR Gene3D; 2.170.170.11; -; 2.
DR HAMAP; MF_00641; Malate_synth_G; 1.
DR InterPro; IPR011076; Malate_synth-like.
DR InterPro; IPR023310; Malate_synth_G_beta_sub_dom.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR006253; Malate_synthG.
DR Pfam; PF01274; Malate_synthase; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01345; malate_syn_G; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Glyoxylate bypass; Magnesium;
KW Metal-binding; Oxidation; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1 742 Malate synthase G.
FT /FTId=PRO_1000056901.
FT REGION 125 126 Acetyl-CoA binding. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT REGION 467 470 Glyoxylate binding. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT ACT_SITE 340 340 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT ACT_SITE 650 650 Proton donor. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT METAL 442 442 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT METAL 470 470 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT BINDING 118 118 Acetyl-CoA; via carbonyl oxygen.
FT {ECO:0000255|HAMAP-Rule:MF_00641}.
FT BINDING 276 276 Acetyl-CoA. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT BINDING 313 313 Acetyl-CoA. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT BINDING 340 340 Glyoxylate. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT BINDING 442 442 Glyoxylate. {ECO:0000255|HAMAP-
FT Rule:MF_00641}.
FT BINDING 551 551 Acetyl-CoA; via carbonyl oxygen.
FT {ECO:0000255|HAMAP-Rule:MF_00641}.
FT MOD_RES 636 636 Cysteine sulfenic acid (-SOH).
FT {ECO:0000255|HAMAP-Rule:MF_00641}.
FT MOD_RES 707 707 Cysteine sulfenic acid (-SOH).
FT {ECO:0000255|HAMAP-Rule:MF_00641}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1 742 ihamap:Malate_synth_G [T]
FT MYHIT 18 716 ipfam:Malate_synthase [T]
SQ SEQUENCE 742 AA; 80564 MW; 52D50E6BAB982917 CRC64;
MTDRTTRHRL QVASQLDRFI NDEALPGTGV DPEAFWAGFD ALVHELVPTN RDLLAERERL
QDELDAWHKA NPGPVRDMAA YRAFLKDIGY LVEAPAKVQA TTANVDDEIA VQAGPQLVVP
VSNARYALNA ANARWGSLYD ALYGTDVIPE TDGAEKSQGY NPKRGEKVIA YARGVLDQAA
PLAEGTHAEA SAYALRDGKL VVTLQGGGET GLADPAQLVG YRGEAQAPTA VLLANHGLHL
EVQFDATHPI GKTDPAHVKD VLVEAAVSTI MDCEDSVAAV DADDKTLVYR NWLGLMKGDL
EERFDKGGKT VTRALNPDRD YTVPGGGELR LPGRSLLFVR NVGHLMTTPA VLDGDGNEIP
EGMLDGVVTS LLAIHDLKKG DGAAPSATAP EAKRNSRTGS VYIVKPKMHG PREVAFANSL
FMRIEDMLGL PRDTLKMGIM DEERRTSINL DACIHEAASR VAFINTGFLD RTGDEMHTAM
EAGPMLRKGE MKGTKWIAAY EKNNVQTGLA CGLRGRAQIG KGMWAMPELM AAMLEQKIGH
PQAGATTAWV PSPTAAVLHA LHYHQVDVAT IQRELEAKPG GDFLDDLLTV PVVESAASGA
NKSPSWSDDE IQQELDNNCQ GILGYVVRWV EHGVGCSKVP DIHDVGLMED RATLRISSQH
IANWLHHGIV SEARVRETLE RMAKVVDDQN AHDPDYTPMT SHLAESCAFQ AASDLIFKGR
EQPAGYTEPL LHHWRAVHKA KS
//
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