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Database: UniProt
Entry: A0A0F5VH70_9GAMM
LinkDB: A0A0F5VH70_9GAMM
Original site: A0A0F5VH70_9GAMM 
ID   A0A0F5VH70_9GAMM        Unreviewed;       591 AA.
AC   A0A0F5VH70;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KKD00830.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:KKD00830.1};
GN   ORFNames=KY46_03160 {ECO:0000313|EMBL:KKD00830.1};
OS   Photobacterium halotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=265726 {ECO:0000313|EMBL:KKD00830.1, ECO:0000313|Proteomes:UP000033633};
RN   [1] {ECO:0000313|EMBL:KKD00830.1, ECO:0000313|Proteomes:UP000033633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MELD1 {ECO:0000313|EMBL:KKD00830.1,
RC   ECO:0000313|Proteomes:UP000033633};
RA   Mathew D.C., Huang C.-C.;
RT   "Mercury Reductase activity and rhizosphere competence traits in the genome
RT   of root associated Photobacterium halotolerans MELD1.";
RL   Submitted (DEC-2014) 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:KKD00830.1}.
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DR   EMBL; JWYV01000002; KKD00830.1; -; Genomic_DNA.
DR   RefSeq; WP_046219196.1; NZ_JWYV01000002.1.
DR   AlphaFoldDB; A0A0F5VH70; -.
DR   STRING; 265726.KY46_03160; -.
DR   PATRIC; fig|265726.11.peg.1975; -.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000033633; 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:KKD00830.1}; Lyase {ECO:0000313|EMBL:KKD00830.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033633};
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..327
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;  64144 MW;  F1A20C6FC2BCFF99 CRC64;
     MAKMKAIEAA VEVLKKEGVI QAFGVPGAAI NPMYAALKKL GGIDHILARH VEGASHMAEG
     YTRTNPGNIG VCIGTSGPAG TDMITGLYSA AADSIPILCI TGQAPRARLH KEDFQAVDIE
     SIAKPVAKWA TTVLEPAQVP RAFQQAFHLM RSGRPGPVLI DLPIDVQLAE IEFDIDSYEP
     LEAYKPTASR AQIEKALTML NQSEKPLIVA GGGVINAGAS DLLQQFAEIT GVPVIPTLMG
     WGSIPDNHEL MVGMVGLQTA HRYGNANMLA SDFVFGVGNR WANRHTGSVD VYTKGRKFVH
     IDIEPTQIGR VFCPDLGIVS DAKAALELIV EVARDMKAAG KLADRSAWVS ECQQRKATML
     RKTHYTETPV KPMRVYEEMN KVFGEETCYV STIGLSQIAA AQFLHVYKPN HWINCGQAGP
     LGWTIPAALG VRAADPQRPV VALSGDYDFQ FMIEELAAGA QFNLPYIHVL VNNSYLGLIR
     QAQRQFDIDY CVQLAFENQN APELNGYGVD HVAVVEGLGC KAIRVTDPEK IADALREAQV
     LMNKHKVPVV VEVILERVTN IAMGVEIDGI NEFEALTEDQ ADAPTAITFN Q
//
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