ID A0A011AHQ7_9ACTN Unreviewed; 564 AA.
AC A0A011AHQ7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:EXG81556.1};
GN ORFNames=CryarDRAFT_2672 {ECO:0000313|EMBL:EXG81556.1};
OS Cryptosporangium arvum DSM 44712.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG81556.1, ECO:0000313|Proteomes:UP000021053};
RN [1] {ECO:0000313|EMBL:EXG81556.1, ECO:0000313|Proteomes:UP000021053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG81556.1,
RC ECO:0000313|Proteomes:UP000021053};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-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:EXG81556.1}.
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DR EMBL; JFBT01000001; EXG81556.1; -; Genomic_DNA.
DR RefSeq; WP_035850917.1; NZ_KK073874.1.
DR AlphaFoldDB; A0A011AHQ7; -.
DR PATRIC; fig|927661.3.peg.2634; -.
DR HOGENOM; CLU_013748_1_2_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000021053; 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: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 Ligase {ECO:0000313|EMBL:EXG81556.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021053};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 61493 MW; C54A1AEAB49FBF48 CRC64;
MPTVPAMQAV VEILESEGVD TVFGCPGAAI LPLYAALQNH GGIEHLIVRH EEGATHMADG
WARTTGNVGV AIGTSGPAGT NMITGLYTAQ ADSIPILCFT GQAVSSKLHQ EAFQAVDIVE
IAKPVTKWAV QVKEAAQVPW IVRKAFQVAR EGRPGPVLVD LPLDVQKELI EWDATIDAPL
PVTPVVPHGP RVERALDLLL SAQRPLILAG GGVILADASA ELRELAEYLQ VPVQVTLMGK
GALDDDHGLH AGMTGIQTSQ RYGNASFLES DLVLAVGARF GDRHTGALDV YRGDRVFIHV
DVEPTQIGKV FGPDLGVVSD ARLFLRALLE AARARHAKRQ PNGWVTRVQH LRRSLTRRED
FDDVPVKAPR VYREINEAFG PDTYFVTAIG LYQIWSGQHQ KVHEPRRYQV CGQAGPLGWE
IPAAIGVKKA APDAEVVGVV GDYSFQFLVE ELAVAAQYDV PFVLIMLNNE YLGLIRQAEL
PYGMNYEVDI HYDAVGTDNV KIMEAYGCSG RRVTRPEEIR DTIEWARKEA ARTSRPALVE
ILIEREANTP HGPAIDAVAE FEPS
//
