ID A0A1Q5N536_9ACTN Unreviewed; 591 AA.
AC A0A1Q5N536;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:OKK21559.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:OKK21559.1};
GN ORFNames=AMK09_13915 {ECO:0000313|EMBL:OKK21559.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK21559.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK21559.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK21559.1,
RC ECO:0000313|Proteomes:UP000186200};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK21559.1}.
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DR EMBL; LIVO01000004; OKK21559.1; -; Genomic_DNA.
DR RefSeq; WP_073735056.1; NZ_LIVO01000004.1.
DR AlphaFoldDB; A0A1Q5N536; -.
DR STRING; 1703920.AMK09_13915; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000186200; 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:OKK21559.1}; Lyase {ECO:0000313|EMBL:OKK21559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186200};
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 591 AA; 63837 MW; A1E44D3B81314AFF CRC64;
MTAARAAVEI LKREGVSNAF GVPGAAINPF YAALKASGGV HHTLARHVEG ASHMAEGYTR
ARPGNIGVCI GTSGPAGTDM ITGLYSAIAD SIPILCITGQ APTAVLHKED FQAVDIASIA
KPVTKAATTV LEAAQVPGVF QQAFHLMRTG RPGPVLIDLP IDVQLTEIEF DPDLYEPLPV
HKPAASRKQI ERALEMLNDS ERPLLVAGGG IINADASELL VEFAELTGVP VVPTLMGWGI
LPDDHELNAG MVGLQTSHRY GNANFLESDF VLGIGNRWAN RHTGKLDVYT QGRKFVHVDI
EPTQLGKIFA PDLGIASDAK AALELFVEVA RELKSAGKLK DRSQWAASTQ ERRATLQRRT
HFDNVPLKPQ RVYEEMNRAF GPDTRYVTTI GLSQIAGAQM LHVYRPRHWI NCGQAGPLGW
TIPAALGVAT ADPEGSVVAL SGDYDFQFML EELAVGAQHN IPYVHVLVNN SYLGLIRQAQ
RNFDIDFQVN LEFENINSPE LGAYGVDHVK VVEGLGCKAI RVTEPDQLLP AFEEAKKLAA
EFRVPVVVEA ILERITNISM SGTDIASVNE FEDVASEPGH APTAIRPFAQ A
//
