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Database: UniProt
Entry: L7L7N8_9ACTN
LinkDB: L7L7N8_9ACTN
Original site: L7L7N8_9ACTN 
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
//
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