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Database: UniProt
Entry: A0A0F0HMK2_9PSEU
LinkDB: A0A0F0HMK2_9PSEU
Original site: A0A0F0HMK2_9PSEU 
ID   A0A0F0HMK2_9PSEU        Unreviewed;       589 AA.
AC   A0A0F0HMK2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KJK56769.1};
DE            EC=4.1.1.47 {ECO:0000313|EMBL:KJK56769.1};
GN   ORFNames=UK12_20675 {ECO:0000313|EMBL:KJK56769.1};
OS   Saccharothrix sp. ST-888.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK56769.1, ECO:0000313|Proteomes:UP000033409};
RN   [1] {ECO:0000313|EMBL:KJK56769.1, ECO:0000313|Proteomes:UP000033409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-888 {ECO:0000313|EMBL:KJK56769.1,
RC   ECO:0000313|Proteomes:UP000033409};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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:KJK56769.1}.
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DR   EMBL; JYJF01000066; KJK56769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0HMK2; -.
DR   PATRIC; fig|1427391.3.peg.6273; -.
DR   Proteomes; UP000033409; 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:KJK56769.1}; Lyase {ECO:0000313|EMBL:KJK56769.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033409};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..118
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          190..324
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          390..549
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   589 AA;  63429 MW;  36FC654130E402AE CRC64;
     MTAARAAVEI LKREGVEVAF GVPGAAINPF YAALKASGGI NHTLARHVEG ASHMAEGYTR
     TKAGNIGVCI GTSGPAGTDM ITGLYSAIAD SIPILCITGQ APVARLHKED FQAVDIASIA
     KPVTKAATTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPEMYEPLPV
     YKPSATRAQI EKAISFLQES ERPLIVAGGG VINADAAELL VEFAELTGTP VVPTLMGWGT
     IPDDHELNAG MVGLQTSHRY GNATLLASDF VLGIGNRWAN RHTGGLDVYT AGRTFVHVDV
     EPTQIGKIFA PDLGIASDAK AALQLFVEVA RELKAAGRLK DRSEWAAATR ERKATLQRKT
     NFDNVPIKPQ RVYQEMNRAF GPETRYVTTI GLSQIAGAQM LHVYKPRHWI NCGQAGPLGW
     TIPAALGVAT ADPEAQVVAL SGDYDFQFMI EELAVGAQHK IPYVHVLVNN SYLGLIRQAQ
     RNFDIDFQVK LEFENLNSPE LGVYGVDHVK VAEGLGCKAI RVTEPDQLLP AFEEAKKLAA
     EFRVPVVVEA ILERVTNISM AGADIDKVNE FEELASRPGD APTAIRPLV
//
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