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
//