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Database: UniProt
Entry: G7ZA96_AZOL4
LinkDB: G7ZA96_AZOL4
Original site: G7ZA96_AZOL4 
ID   G7ZA96_AZOL4            Unreviewed;       589 AA.
AC   G7ZA96;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:CBS88594.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:CBS88594.1};
GN   Name=gcl {ECO:0000313|EMBL:CBS88594.1};
GN   OrderedLocusNames=AZOLI_p10310 {ECO:0000313|EMBL:CBS88594.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88594.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88594.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p1 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; FQ311869; CBS88594.1; -; Genomic_DNA.
DR   RefSeq; WP_014188051.1; NC_016585.1.
DR   AlphaFoldDB; G7ZA96; -.
DR   KEGG; ali:AZOLI_p10310; -.
DR   HOGENOM; CLU_013748_1_3_5; -.
DR   OMA; TLMGWGA; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p1.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009028; F:tartronate-semialdehyde synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009436; P:glyoxylate catabolic process; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR006397; Glyox_carbo_lig.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR01504; glyox_carbo_lig; 1.
DR   PANTHER; PTHR18968:SF14; GLYOXYLATE CARBOLIGASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000313|EMBL:CBS88594.1}; Lyase {ECO:0000313|EMBL:CBS88594.1};
KW   Plasmid {ECO:0000313|EMBL:CBS88594.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..552
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   589 AA;  64733 MW;  C3F55A9764F841C5 CRC64;
     MARMTAAEAA VRVLEREGID VCFGVPGAAI NPFYAAMQRR GTMRHVLARH VEGASHMAEG
     YTRARAGNIG VCVGTSGPAG TDMITGLYSA IADSIPILCI TGQAPRARLH KEDFQAINVP
     DIARPVTKWA LTVLEPAQVP YVFQQAFHLM RSGRPGPVLI DLPIDVQMAE IEFDDETYEP
     LPVYKPSATR AQVEKALAMF AAAERPLVVA GGGIINADAS DKLVEFAELL GVPVIPTLMG
     WGTIPDDHPL MAGMVGLQTA HRYGNATMLK SDFVLGIGNR WANRHTGSVE VYTKGRKFVH
     VDIEPTQIGR VFMPDLGIVS DAGAALDMFI EVAKEWKAEG RFKDLGGWVR DCQGRKRSMH
     RRSDFDQVPM KPQRVYQEMN SAFGQDTTYV TTIGLSQIAG AQFLHVYKPR HWINCGQAGP
     LGWTLPAALG VRVADPQRRI VALSGDYDFQ FMIEELAVGA QHKLPYIHVL VNNAYLGLIR
     QAQRAFQMDF QVQLSFENIN APEIGVYGVD HVAVAEGLGC KAIRVTEPDR IQDAFAQAQA
     WMDEYRVPVV VELVLERVTN IAMGTDIDSV NEFEEILDLP VEESETVLV
//
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