(data stored in SCRATCH zone)

SWISSPROT: C1ASU9_RHOOB

ID   C1ASU9_RHOOB            Unreviewed;       726 AA.
AC   C1ASU9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 69.
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:BAH48881.1};
GN   Synonyms=aceB {ECO:0000313|EMBL:BAH48881.1};
GN   OrderedLocusNames=ROP_06340 {ECO:0000313|EMBL:BAH48881.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48881.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48881.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48881.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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:0000256|HAMAP-Rule:MF_00641, ECO:0000256|SAAS:SAAS00078445}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + glyoxylate = (S)-malate +
CC       CoA. {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00378410}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00641, ECO:0000256|SAAS:SAAS00171973};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate
CC       from isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00378382}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
CC       ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078437}.
CC   -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572,
CC       ECO:0000256|SAAS:SAAS00559604}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP011115; BAH48881.1; -; Genomic_DNA.
DR   RefSeq; WP_012687886.1; NC_012522.1.
DR   STRING; 632772.ROP_06340; -.
DR   EnsemblBacteria; BAH48881; BAH48881; ROP_06340.
DR   KEGG; rop:ROP_06340; -.
DR   PATRIC; fig|632772.20.peg.694; -.
DR   eggNOG; ENOG4107QP3; Bacteria.
DR   eggNOG; COG2225; LUCA.
DR   HOGENOM; HOG000220740; -.
DR   KO; K01638; -.
DR   OMA; GDEMHTS; -.
DR   OrthoDB; POG091H05P0; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000002212; 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   HAMAP; MF_00641; Malate_synth_G; 1.
DR   InterPro; IPR011076; Malate_synth-like.
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;
DR   PRODOM; C1ASU9.
DR   SWISS-2DPAGE; C1ASU9.
KW   Acyltransferase {ECO:0000313|EMBL:BAH48881.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00078450};
KW   Glyoxylate bypass {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078429};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00078439};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|SAAS:SAAS00078435};
KW   Oxidation {ECO:0000256|HAMAP-Rule:MF_00641};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00455574,
KW   ECO:0000313|EMBL:BAH48881.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00641,
KW   ECO:0000256|RuleBase:RU003572, ECO:0000256|SAAS:SAAS00078455}.
FT   REGION      124    125       Acetyl-CoA binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00641}.
FT   REGION      459    462       Glyoxylate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00641}.
FT   ACT_SITE    339    339       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641, ECO:0000256|PIRSR:PIRSR601465-
FT                                50}.
FT   ACT_SITE    633    633       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641, ECO:0000256|PIRSR:PIRSR601465-
FT                                50}.
FT   METAL       434    434       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   METAL       462    462       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     117    117       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
FT   BINDING     275    275       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     312    312       Acetyl-CoA. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     339    339       Glyoxylate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     434    434       Glyoxylate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00641}.
FT   BINDING     543    543       Acetyl-CoA; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
FT   MOD_RES     619    619       Cysteine sulfenic acid (-SOH).
FT                                {ECO:0000256|HAMAP-Rule:MF_00641}.
SQ   SEQUENCE   726 AA;  78776 MW;  B67EA5B820EB0E22 CRC64;
     MTERVEVGGL QVAKVLYDFV NEEALPGTGI DVDGFWSGAV KVIEDLAPRN RSLLAVRDDL
     QARIDTWHRD HTGTPDPAEY RQFLTSIGYL VPEPGPFAVS TANVDAEITS TAGPQLVVPV
     LNARFALNAA NARWGSLYDA LYGTNAIGVD GGAEPGDSYN RVRGDRVIAW ARNFLDTAAP
     LRSGSHADAA RYTVDGGALA VALADGTSTG LADPGKFVGY LGDPAAPSSV LLRNHGLHAE
     IQIDPTSPIG QTDAAGVQDV VLESAVTTIM DFEDSVAAVD ADDKVIGYRN WLGLNRGDLT
     EELTKGGQAF TRRLNPDRTY TAPDGGELTL HGRSLLFVRN VGHLMSTPAI LHPDGTEIPE
     GILDALLTSL CAIHGLSRSE QTGPLDNSRT GSIYIVKPKQ HGPDEVAFTT DLFGRVEQVL
     NLPANTIKVG IMDEERRTTV NLAACIHEAR ERVVFINTGF LDRTGDEIHT SMEAGPMIRK
     AEMKQQTWIS AYEDWNVDIG LACGLQGRAQ IGKGMWAMTE LMAEMLEQKI GHPKAGANTA
     WVPSPTGATL HATHYHQVDV FAVQDELKGT RRAGLDQILT IPLAPDTDWT EEQKQEELDN
     NCQSILGYVV RWIDAGVGCS KVPDIHDVAL MEDRATLRIS SQLLANWIRH GVVTAEQVVA
     SLQRMAPVVD RQNQGDPTYR PLAPDFDTNI AFQAAKELIL DGTTQPSGYT EPILHRRRRE
     YKAANA
//

If you have problems or comments...

PBIL Back to PBIL home page