ID A0A022MQS6_9ACTN Unreviewed; 591 AA.
AC A0A022MQS6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:EYT83100.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:EYT83100.1};
GN ORFNames=CF54_09355 {ECO:0000313|EMBL:EYT83100.1};
OS Streptomyces sp. Tu 6176.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT83100.1, ECO:0000313|Proteomes:UP000020060};
RN [1] {ECO:0000313|EMBL:EYT83100.1, ECO:0000313|Proteomes:UP000020060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT83100.1,
RC ECO:0000313|Proteomes:UP000020060};
RA Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT cytotoxic benzoxazol nataxazol.";
RL Submitted (MAR-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:EYT83100.1}.
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DR EMBL; JFJQ01000284; EYT83100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022MQS6; -.
DR HOGENOM; CLU_013748_1_3_11; -.
DR Proteomes; UP000020060; 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:EYT83100.1}; Lyase {ECO:0000313|EMBL:EYT83100.1};
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; 63482 MW; 3B1B4D177295C957 CRC64;
MTAARAAVEI LKREGVTDAF GVPGAAINPF YAALKASGGI GHTLARHVEG ASHMAEGYTR
THPGNIGVCI GTSGPAGTDM ITGLYSAIGD SIPILCITGQ APTAVIHKED FQAVDIASIA
KPVTKMAVTV LEAAQVPGVF QQAFHLMRSG RPGPVLIDLP IDVQLTEIEF DPDTYEPLPV
YKPAASRAQI EKAIGMLTAA ERPLIVAGGG IINADATDLL VEFAELTGTP VVPTLMGWGI
LPDDHELNAG MVGLQTSHRY GNATFLESDF VLGIGNRWAN RHTGKLDVYT AGRTFVHVDV
EPTQIGKIFA PDYGIASDAK AALKLFVEVA RELKAAGKLP DRSAWAAAAQ ERKATLQRRT
HFDDIPIKPQ RVYEEMNKAF GPETRYVSTI GLSQIAGAQM LHVYRPRHWI NCGQAGPLGW
TVPAALGVAK ADPESPVVAL SGDYDFQFML EELAVGAQHR IPYIHVLVNN SYLGLIRQAQ
RAFDIDFQVK LEFENINAPE LGVYGVDHVR VAEGLGCKAI RVTDPNELGA AFEEAKKLAA
EHRVPVVVEA ILERVTNISM SGTNDISNVV EFEELATEPQ HAPTALKPLK V
//
