ID A0A084A0L0_9GAMM Unreviewed; 579 AA.
AC A0A084A0L0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glyoxylate carboligase {ECO:0000313|EMBL:KEY58839.1};
DE EC=4.1.1.47 {ECO:0000313|EMBL:KEY58839.1};
GN Name=gcl_2 {ECO:0000313|EMBL:KEY58839.1};
GN ORFNames=SRDD_22290 {ECO:0000313|EMBL:KEY58839.1};
OS Serratia sp. DD3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY58839.1, ECO:0000313|Proteomes:UP000017810};
RN [1] {ECO:0000313|EMBL:KEY58839.1, ECO:0000313|Proteomes:UP000017810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD3 {ECO:0000313|EMBL:KEY58839.1,
RC ECO:0000313|Proteomes:UP000017810};
RX PubMed=25212623;
RA Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT of Daphnia magna.";
RL Genome Announc. 2:e00903-14(2014).
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:KEY58839.1}.
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DR EMBL; AYKS02000063; KEY58839.1; -; Genomic_DNA.
DR RefSeq; WP_023490248.1; NZ_AYKS02000063.1.
DR AlphaFoldDB; A0A084A0L0; -.
DR STRING; 1410619.SRDD_22290; -.
DR eggNOG; COG3960; Bacteria.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000017810; 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:KEY58839.1}; Lyase {ECO:0000313|EMBL:KEY58839.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..553
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 63222 MW; 7F23CA1E5CBA0966 CRC64;
MARMRATEAA VQILKKEGIS VAFGVPGAAI NPLYAALKKL GGIDHILARH VEGASHMAEG
YTRAAPDNIG LCIGTSGPAG TDMITGLYSA SADSIPILCI TGQAPVAKLH KEDFQSVDIE
SIAKPVTKMA VTVLEAGQLP GTLQKAFFEM RSGRPGPVLI DLPFDVQMTE IEFDIDLYQP
MVPHRPQATR AQAVRALEMM NDAEKPVVIA GGGIINAEAS DLLQQLAEVT GVPVIQTLRG
WGSIPDDHPL MAGRMGCQAN HRYGNANFLE SDFVFGIGNR WANRNTGALD TYTKGRKFIH
VDIEPTQIGR VFSPDLGIVS DAKAALIQLV EVAKEMQAAG KLKDRSAWAE SCLLRKRSMQ
RRDDFDCTPI KPQRIYHEMN KAFGKETRYI ATIGLAQIAA NQFLHVYKPR NWINACQAGP
LGWTLPAALG VVKADPQAQV VAISGDYDFQ FLVEELAVGA QFNLPYIHVL INNAYLGLIR
QAQRAFDIDY CVQLAFENIN APELNGYGVD HLKVVEGLGC KALRVFDPAM IGPALEEAKQ
LRDRYRVPVV VEVITERVTN IAMGPDIDKV TEFEEIIDL
//