ID A0A061LX30_9MICO Unreviewed; 546 AA.
AC A0A061LX30;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=5-guanidino-2-oxopentanoate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=H490_0104220 {ECO:0000313|EMBL:EYT55831.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT55831.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT55831.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT55831.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(2013).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EYT55831.1}.
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DR EMBL; APJM01000007; EYT55831.1; -; Genomic_DNA.
DR RefSeq; WP_017883527.1; NZ_KB714601.1.
DR AlphaFoldDB; A0A061LX30; -.
DR STRING; 1292023.H490_0104220; -.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000026917; 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; cd00568; TPP_enzymes; 1.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000026917};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..305
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 57990 MW; 75F2433817ADDF81 CRC64;
MRLGQAISSL LTEYGIEQIF GIPGVHTLEL FRDIDRSGLR VTIPRHEQGA GFMADAYTRV
SGIPGVCYLI TGPGVLNALT PIAQAWHDSI PMLVIGSTVT RDQLGEHRGT LHDTPDLAEV
LRPFTLISET ATSAERVAEL IDEAFRRWEH ERARPVYIGV PRDLLEEEVG EPHRPAPRAA
LPPAAETEEI SARLVEALDR LASSDRPVIV AGGGARHDGA AVTRLAERLA APVVLTGNAK
GLIADEHPLN VGISMPFPRT QELLEDADLV VALGTELSDF EFLFTGSPEP RLADIVRVDI
DPQTTHPDQT RPTLPMRVAD FARTALAGLE EPNAAASAAG AARAATAKSG LAEAREADPH
TPWIDAIERA LPESAILTAD SAQVAYQSHH FLSLHGPGRW LAPYGYGTLG PALPMAIGAA
IAAPGRPVIG LAGDGSSLFT LPELATAHDL GANITLVIWD NGGYREIEIS FDRTDIQPAG
VRTSAHDLGA IAAGFGAEVT RATTPAELED ALREATARPA LSVIVVRAPA EHRVEADSLL
REGADA
//