ID A0A077FHY0_9PSED Unreviewed; 591 AA.
AC A0A077FHY0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:AIL62841.1};
GN ORFNames=PSAKL28_36890 {ECO:0000313|EMBL:AIL62841.1};
OS Pseudomonas alkylphenolica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL62841.1, ECO:0000313|Proteomes:UP000028931};
RN [1] {ECO:0000313|EMBL:AIL62841.1, ECO:0000313|Proteomes:UP000028931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KL28 {ECO:0000313|EMBL:AIL62841.1,
RC ECO:0000313|Proteomes:UP000028931};
RA Lee K., Lim J.Y., Hwang I.;
RL Submitted (JUL-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; CP009048; AIL62841.1; -; Genomic_DNA.
DR RefSeq; WP_038613253.1; NZ_CP009048.1.
DR AlphaFoldDB; A0A077FHY0; -.
DR KEGG; palk:PSAKL28_36890; -.
DR eggNOG; COG3960; Bacteria.
DR HOGENOM; CLU_013748_1_3_6; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000028931; Chromosome.
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:AIL62841.1};
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; 64236 MW; 3ACD206EFAC74045 CRC64;
MSKMRAIDAA VLVMRREGVE TAFGIPGAAI NPLYSALKKV GGIDHVLARH VEGASHMAEG
YTRTKAGNIG VCIGTSGPAG TDMVTGLYSA SADSIPILCI TGQAPRARMH KEDFQAVDIT
SIVKPVTKWA TTVLEPGQVP YAFQKAFYEM RSGRPGPVLI DLPFDVQMAE IEFDIDAYQP
LPVHKPAANR IQVEKALAML DTAERPLLVA GGGIINADAC DKLVEFAELT GIPVIPTLMG
WGIIPDDHPL MVGMVGLQTS HRYGNATMLK SDVVLGIGNR WANRHTGSVD VYTEGRRFIH
VDIEPTQIGR VFTPDLGIVS DAGAALDVFL EVAREWKAAG KLKDRSAWLE DCQQRKSSLQ
RKTHFDNVPV KPQRVYQEMN QVFGKDTCYV STIGLSQIAG AQFLHVYKPR HWINCGQAGP
LGWTIPAALG VVKADPTRKV VALSGDYDFQ FMIEELAVGA QFNLPYVHVL VNNSYLGLIR
QAQRGFEMDY CVQLAFENVN APELNGYGVD HVAVVEGLGC KALRVTEPGE IAPALLKAQK
LAEEFRVPVV VEVILERVTN ISMGTEINAV NEFEDLALVG NDAPTAISLL D
//