ID   C9QF50_VIBOR            Unreviewed;       591 AA.
AC   C9QF50;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:EGU51459.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:EGU51459.1};
GN   ORFNames=VIOR3934_21341 {ECO:0000313|EMBL:EGU51459.1};
OS   Vibrio orientalis CIP 102891 = ATCC 33934.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU51459.1, ECO:0000313|Proteomes:UP000002817};
RN   [1] {ECO:0000313|EMBL:EGU51459.1, ECO:0000313|Proteomes:UP000002817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102891 / ATCC 33934 {ECO:0000313|Proteomes:UP000002817};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU51459.1}.
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DR   EMBL; AFWH01000018; EGU51459.1; -; Genomic_DNA.
DR   RefSeq; WP_004412806.1; NZ_AFWH01000018.1.
DR   AlphaFoldDB; C9QF50; -.
DR   STRING; 675816.VIA_001920; -.
DR   PATRIC; fig|675816.5.peg.1631; -.
DR   eggNOG; COG3960; Bacteria.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000002817; 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: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:EGU51459.1}; Lyase {ECO:0000313|EMBL:EGU51459.1};
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;  64640 MW;  D361BD6BA43F7115 CRC64;
     MAKMKAIEAA VEVLKKEGVD IAFGVPGAAI NPMYAAMKKL GGIDHVLARH VEGASHMAEG
     YTRTNQDNIG VCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPRARLH KEDFQAVDIE
     SIAKPVTKWA TTVLEPAQVP RAFQQAFHLM RSGRPGPVLI DLPLDVQLTE IEFDIDTYEP
     LEAYQPKATR AQVEKAMEMM CESANPLIVS GGGVINAGAE ELLQQFAEIT GVPVVPTLMG
     WGSIADDHEL MAGMVGLQTS HRYGNATMLE SDFVFGIGNR WANRHTGSLD VYTKGRKFVH
     VDIEPTQIGR VFCPDLGIVS DAKAALELLV EVAREWRDAG KLPNRSTWVG ECQQRKATML
     RKTHYTDAPI KPMRVYEEMN KAFDRDTCYV STIGLSQIAA AQFLHVYKPR HWINCGQAGP
     LGWTTPAALG VRAADPNRDI VAISGDYDFQ FMIEELAVGA QFNLPYIHVL VNNSYLGLIR
     QAQRQFDIDY CVQLAFENQN APELNGYGVD HVTVVEGLGC KAIRVTDPEQ MQAAFAEAKE
     LMNKHKVPVV VEVILERVTN IAMGVEINAI NEFEALAENA DDAPTALIHR G
//