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
//