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
//