ID A0A1C0AM80_9ACTN Unreviewed; 730 AA.
AC A0A1C0AM80;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
GN Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641};
GN ORFNames=BCR15_04145 {ECO:0000313|EMBL:OCL33998.1};
OS Tessaracoccus lapidicaptus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1427523 {ECO:0000313|EMBL:OCL33998.1, ECO:0000313|Proteomes:UP000093501};
RN [1] {ECO:0000313|Proteomes:UP000093501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPBSL-7 {ECO:0000313|Proteomes:UP000093501};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the
CC condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-
CC CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP-
CC Rule:MF_00641}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+);
CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001699, ECO:0000256|HAMAP-
CC Rule:MF_00641, ECO:0000256|RuleBase:RU003572};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00641};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC ECO:0000256|RuleBase:RU003572}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC ECO:0000256|RuleBase:RU003572}.
CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
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:OCL33998.1}.
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DR EMBL; MBQD01000021; OCL33998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0AM80; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000093501; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.360; Malate synthase, domain 3; 2.
DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
DR HAMAP; MF_00641; Malate_synth_G; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR001465; Malate_synthase_TIM.
DR InterPro; IPR006253; Malate_synthG.
DR InterPro; IPR048355; MS_C.
DR InterPro; IPR048356; MS_N.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR InterPro; IPR048357; MSG_insertion.
DR NCBIfam; TIGR01345; malate_syn_G; 1.
DR PANTHER; PTHR42739; MALATE SYNTHASE G; 1.
DR PANTHER; PTHR42739:SF1; MALATE SYNTHASE G; 1.
DR Pfam; PF20659; MS_C; 1.
DR Pfam; PF20656; MS_N; 1.
DR Pfam; PF01274; MS_TIM-barrel; 1.
DR Pfam; PF20658; MSG_insertion; 1.
DR SUPFAM; SSF51645; Malate synthase G; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641};
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641};
KW Reference proteome {ECO:0000313|Proteomes:UP000093501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00641};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00641}.
FT DOMAIN 17..76
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 160..234
FT /note="Malate synthase G alpha-beta insertion"
FT /evidence="ECO:0000259|Pfam:PF20658"
FT DOMAIN 336..578
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 591..680
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 631
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT BINDING 118
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 125..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 275
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 312
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 339
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 431
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 431
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 456..459
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 540
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT MOD_RES 617
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
SQ SEQUENCE 730 AA; 80449 MW; 5A74DA8C0A793CB8 CRC64;
MHATHAPVGR LWVDRTLVDF LDREALPVAG VDRERFWAGF EEVFDRFTGR NRALLEERRR
LQQAINEFHR AHPGRPDAGH YRSFLTRIGY LLPEATEVAA RTTGVDREIA EVAGPQLVVP
VTNRRFAINA ANARWGSLYD ALYGTDVIDD GDGAGREGRY NPVRGAKVIA WAREFLDAVA
PLASGSHTDV AGYRAGRVFE AMLSSGQIVG LADPDTYAGF QGEPGAPDAI LLAHHGLHLE
LRIDRQGRIG REDPAGIDDI VLESAVTAIM DFEDSVATVD GPDKVVAYRT WLQLNDGTAI
EEMSKGGRQF TRTLADDRRF TRPDGTELRL PGRALMLCRN VGHLMTTPAV LDDEGQELPE
GILDALVTSL CAMPGLRADA RRANSRTGSI YIVKPKQHGP DEVAFTSDLF AAVEDVLGLP
RTTLKMGIMD EERRTTVNLA ACIAQAADRI IFINTGFLDR TGDEIHTSME AGPMIRKAEM
KQAAWMRAYE DWNVDVGIAC GLPGRAQIGK GMWAKTDLMA EMVAEKIGHP ASGATTAWVP
SPTAATLHAT HYHRVDARER QAGIAAGGGR ATRDDLLEIP LATSTRWSPE ERQEEVDNSC
QSILGYVVRW IDQGVGCSKV PDITDTSLME DRATCRISSQ MLANWIRHGI VSEQYVLQSL
KRMAAVVDAQ NAGDRTYRPM TPREGGSFED SIAWCAARDL VVQGTWSPSG YTEPILHRRR
REYKARYRLS
//
