ID   Q1YZT6_9GAMM            Unreviewed;       591 AA.
AC   Q1YZT6;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   SubName: Full=Putative glyoxylate carboligase {ECO:0000313|EMBL:EAS41789.1};
GN   ORFNames=P3TCK_01205 {ECO:0000313|EMBL:EAS41789.1};
OS   Photobacterium profundum 3TCK.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS41789.1, ECO:0000313|Proteomes:UP000003789};
RN   [1] {ECO:0000313|EMBL:EAS41789.1, ECO:0000313|Proteomes:UP000003789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3TCK {ECO:0000313|EMBL:EAS41789.1,
RC   ECO:0000313|Proteomes:UP000003789};
RA   Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA   Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:EAS41789.1}.
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DR   EMBL; AAPH01000029; EAS41789.1; -; Genomic_DNA.
DR   RefSeq; WP_006233614.1; NZ_CH724138.1.
DR   AlphaFoldDB; Q1YZT6; -.
DR   HOGENOM; CLU_013748_1_2_6; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000003789; Unassembled WGS sequence.
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:InterPro.
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:EAS41789.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..120
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;  64369 MW;  578705B771E2AD28 CRC64;
     MARMTAIEAA IEVLKREGVD IAFGVPGAAI NPMYAAMKKL GGIDHVLARH VEGASHMAEG
     YTRTSQGNIG VCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE
     TIAKPVTKWA TTVLEPAQVP RAFQKAFHLM RSGRPGPVLI DLPIDVQLTE IEFDIDSYEP
     LDAYKPTASR AQVEKAITML NDARNPVIVS GGGVINAGAS TLLQQFAEIT GIPVIPTLMG
     WGSIPDNHEL MAGMVGLQTA HRYGNATLLG SDFVLGIGNR WANRHTGSID VYTEGRKFVH
     IDIEPTQIGR VFCPDLGIVS DAKAALELLV EVAREWKQAG KLKDRCDWAG ECQHRKSTML
     RKTHFDEVPM KPMRVYEEMN KAFDEDTCYV STIGLSQIAA AQFLHVYKPR HWINCGQAGP
     LGWTIPAALG VRAADPDRPI VAISGDYDFQ FMIEELAVGA QFNLPYIHVV VNNSYLGLIR
     QAQRQFDIDY CVQLAFDNQN APELEGYGVD HVAVVEGLGC KAIRVRDPDQ VGNAFAQAKE
     LMVKHKVPVV VEIMLERVTN ISMGVEINGV NEFEPLAEGS ADAPTAITFN Q
//