ID R2XVT1_9ENTE Unreviewed; 556 AA.
AC R2XVT1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Glyoxylate carboligase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UKC_00225 {ECO:0000313|EMBL:EOI59039.1};
OS Enterococcus gilvus ATCC BAA-350.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI59039.1, ECO:0000313|Proteomes:UP000013750};
RN [1] {ECO:0000313|EMBL:EOI59039.1, ECO:0000313|Proteomes:UP000013750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI59039.1,
RC ECO:0000313|Proteomes:UP000013750};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL Submitted (FEB-2013) 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:EOI59039.1}.
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DR EMBL; AJDQ01000002; EOI59039.1; -; Genomic_DNA.
DR AlphaFoldDB; R2XVT1; -.
DR PATRIC; fig|1158614.3.peg.216; -.
DR eggNOG; COG3960; Bacteria.
DR HOGENOM; CLU_013748_1_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000013750; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; 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; 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 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 188..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 556 AA; 60544 MW; 33E2A0FED12C2BDA CRC64;
MKAADAIVQI MVKEGITDAF GIPGAGINPV YKYLEEAPIE HFCMRHEEAC MHAADGYYRA
SHKISAALCT SGPGATNFVT GLYTAQIDSI PVLAITGQAN SWQMKQDAFQ CVDMESIAKT
VCKKVFCVLE AEKIPEIMQE AFYLMRNGKP GPVLLDLPLD IQQTDIDFDI ADYQPAAKET
VTPEAAKIQQ AMDMIQKANA PIIVMGGGVI LSHAEKELIA FAEMLEIPVI TTYMAKGGLP
EEHPLNAGHA GIQVGQPIGN RYFLDSDVVI GIGNRFTDRH TGNLAVYREG RQFIHIDIEK
GQIGKVFEPE LGIVSDAKEA LIALIAEAKA RNVKPINSQR AADLPATRKE LARKTDFDSK
PMMPHRVFHE MNAAFDDATM FTAGCGITQI WSGQLQKINR ARRYLPSGGA GTLGYEVPAA
FGAKVADPAA HSVTVLGDFG FTFMGEEIAV AAAFKKPIIV IIVNNAYLGL IRQNQKGAYG
FEYAVDMPYN QDGTMDYVKV AEGFGCVGER VFTPDELRGA IDRAKQSNKT YVIDAICKPE
QLCDMGTALD NVKSFV
//