ID A0A101KS89_RHILI Unreviewed; 526 AA.
AC A0A101KS89;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=5-guanidino-2-oxopentanoate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AU467_23495 {ECO:0000313|EMBL:KUM25965.1};
OS Rhizobium loti (Mesorhizobium loti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=381 {ECO:0000313|EMBL:KUM25965.1, ECO:0000313|Proteomes:UP000053176};
RN [1] {ECO:0000313|EMBL:KUM25965.1, ECO:0000313|Proteomes:UP000053176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM25965.1,
RC ECO:0000313|Proteomes:UP000053176};
RA Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT efficient symbiont and plant-growth promoting strain isolated from Zn-
RT mining soil using Leucaena leucocephala as a trap plant.";
RL Submitted (DEC-2015) 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:KUM25965.1}.
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DR EMBL; LPWA01000110; KUM25965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101KS89; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000053176; 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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 526 AA; 54113 MW; 8E92602355662E23 CRC64;
MTTVGEALIT LLEAHGVDTV FGIPGVHTVE LYRGLARSKI RHVTPRHEQG AGFMADGYAR
VSGRPGVAFV ITGPGLTNTI TAMGQARADS VPMLVISGVN ATDTLGKGLG FLHELPDQRG
MMEKVALFSE RVTEAGELPG ALARAFTVFS SSRPGPVHIE IPTDVMVKPA EGIAPVLSNA
APPAPASAAI ADAVKLIKTA RRPLILVGGG AKRADAALTR FAEALGAPVV ETANARGLLH
GHPLCVPASP SLKAVRVLMA DADLVIAAGT EFGPTDYDGY GDGGFVLPPN LIRIDIGADQ
LARRPVTVGI QADCAEALGA LLAELGSAHD AAKDGEARAA AGREAALAEL RPEYVAQVRA
VEAIRGALPG AIIVGDSTQP IYAANLYYDH DRPGGWFNAA TGFGALGYGP PAAIGAALAM
PEAPVVCLTG DGGFQFTLPE LGAALDAGAP VIFVVWNNRG YREIETSMLD VGVEPVGVSP
APPDFCKLAE AYGIEAERLT GVGGLADALK RARAAGKPRL VEITVD
//
