ID L7L7N8_9ACTN Unreviewed; 738 AA.
AC L7L7N8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 ECO:0000313|EMBL:GAC56052.1};
GN ORFNames=GOHSU_02_01990 {ECO:0000313|EMBL:GAC56052.1};
OS Gordonia hirsuta DSM 44140 = NBRC 16056.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC56052.1, ECO:0000313|Proteomes:UP000053405};
RN [1] {ECO:0000313|EMBL:GAC56052.1, ECO:0000313|Proteomes:UP000053405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC56052.1,
RC ECO:0000313|Proteomes:UP000053405};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056.";
RL Submitted (DEC-2012) 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:GAC56052.1}.
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DR EMBL; BANT01000002; GAC56052.1; -; Genomic_DNA.
DR RefSeq; WP_005935465.1; NZ_BANT01000002.1.
DR AlphaFoldDB; L7L7N8; -.
DR STRING; 1121927.GOHSU_02_01990; -.
DR eggNOG; COG2225; Bacteria.
DR OrthoDB; 9762054at2; -.
DR UniPathway; UPA00703; UER00720.
DR Proteomes; UP000053405; 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 CDD; cd00728; malate_synt_G; 1.
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:UP000053405};
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 16..76
FT /note="Malate synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20656"
FT DOMAIN 159..241
FT /note="Malate synthase G alpha-beta insertion"
FT /evidence="ECO:0000259|Pfam:PF20658"
FT DOMAIN 343..582
FT /note="Malate synthase TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01274"
FT DOMAIN 596..695
FT /note="Malate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20659"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT ACT_SITE 636
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641,
FT ECO:0000256|PIRSR:PIRSR601465-50"
FT BINDING 117
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 124..125
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 282
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 319
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 346
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 437
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 437
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 462..465
FT /ligand="glyoxylate"
FT /ligand_id="ChEBI:CHEBI:36655"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT BINDING 546
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
FT MOD_RES 622
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641"
SQ SEQUENCE 738 AA; 80449 MW; DF3C5251A9FDCF5F CRC64;
MTERVTVDGL QVASELYEFV NNEALPGTGV EPAAFWSGAA AIINDLAPRN RELLAVRDEL
QTKIDQWHRD NPGAVDQDAY IAFLKEIGYL VDPPADFEIT TANVDTEITE TAGPQLVVPI
LNARFALNAS NARWGSLYDA LYGTDVIPET DGAEKGTSYN KVRGDKVIAF AKNFLDKAFP
LESGSHTDAT RYVVDGDKVN VTLGNLAEGG KDIEVTTFAD PAAFVGYTGD ATDPSAILLR
HHGLHAEIQF DAASPIGATD AANIKDVALE SAVTTIMDFE DSVAAVDAED KVLGYRNWLG
LNKGDLTEQV TKNGKTFTRV LNPNRVYTGR DGKPVELHGR SLLFVRNVGH LMTNPAILDA
EGNEVPEGIL DALITSAVAI HGMSPEGMQN SRTGSVYIVK PKMHGPDEVA FTVELFGRVE
DVLGLPRNTL KVGIMDEERR TTANLKAAIH NASERVVFIN TGFLDRTGDE IHTSMEAGPM
VRKADMKQQT WIKAYEDWNV DTGLAAGLQH KAQIGKGMWA MPNLMADMLE QKIAHPSAGA
NTAWVPSPTA ATLHALHYHD VDVFERQNEI AKREPAKLED ILTIPLAADP NWTDEQKREE
LDNNCQSILG YVVRWIDQGV GCSTVPDIHD VGLMEDRATL RISSQLLANW LRHGVVSEDD
VIAALERMAP VVDRQNAGDP LYTPMAPDFD DSIAFQASKA LILEGAAQPS GYTEPILHKA
RQDAKAARRT QVVSPRLI
//