ID F9TAW1_9VIBR Unreviewed; 591 AA.
AC F9TAW1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AIW17039.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:AIW17039.1};
GN ORFNames=IX91_23455 {ECO:0000313|EMBL:AIW17039.1};
OS Vibrio tubiashii ATCC 19109.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW17039.1, ECO:0000313|Proteomes:UP000030071};
RN [1] {ECO:0000313|EMBL:AIW17039.1, ECO:0000313|Proteomes:UP000030071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW17039.1,
RC ECO:0000313|Proteomes:UP000030071};
RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT tubiashii.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP009355; AIW17039.1; -; Genomic_DNA.
DR RefSeq; WP_004747386.1; NZ_CP009355.1.
DR AlphaFoldDB; F9TAW1; -.
DR STRING; 1051646.IX91_23455; -.
DR GeneID; 78077692; -.
DR KEGG; vtu:IX91_23455; -.
DR PATRIC; fig|1051646.9.peg.4620; -.
DR eggNOG; COG3960; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR Proteomes; UP000030071; Chromosome 2.
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:AIW17039.1}; Lyase {ECO:0000313|EMBL:AIW17039.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 591 AA; 64357 MW; 4391CCAAA2021AFD CRC64;
MAKMKAIEAA VEVLKKEGVD IAFGVPGAAI NPMYAAMKKL GGIDHVLARH VEGASHMAEG
YTRTNQGNIG VCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE
SIAKPVTKWA TTVLEPAQVP RAFQQAFHLM RSGRPGPVLI DLPLDVQLTE IEFDIDTYEP
LEAYQPKATR AQVEKAIEMM CESANPVIVS GGGVINAGAE ALLQQFAEIT GVPVIPTLMG
WGSIADDHEL MAGMVGLQTA HRYGNATLLE SDFVFGIGNR FANRHTGSLD VYTKGRKFVH
VDIEPTQIGR VFCPDLGIVS DAKAALELLV EVAREWRDAG KLPNRSAWVG ECQQRKATML
RKTHYTDAPI KPMRVYEEMN KAFGRDTCYV STIGLSQIAA AQFLHVYKPR HWINCGQAGP
LGWTTPAALG VRAADPNRDI VAISGDYDFQ FMIEELAVGA QFNLPYIHVL VNNSYLGLIR
QAQRQFDIDY CVQLAFENQN APELNGYGVD HVTVVEGLGC KAIRVTDPEQ MQEAFAQAKE
LMNKHKVPVV VEVILERVTN IAMGVEIDSI NEFEALAESA DDAPTALINN S
//
