ID A0A0T6UMI1_9PSED Unreviewed; 534 AA.
AC A0A0T6UMI1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=5-guanidino-2-oxopentanoate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AO726_14720 {ECO:0000313|EMBL:KRW58770.1};
OS Pseudomonas sp. TTU2014-080ASC.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1729724 {ECO:0000313|EMBL:KRW58770.1, ECO:0000313|Proteomes:UP000051864};
RN [1] {ECO:0000313|EMBL:KRW58770.1, ECO:0000313|Proteomes:UP000051864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTU2014-080ASC {ECO:0000313|EMBL:KRW58770.1,
RC ECO:0000313|Proteomes:UP000051864};
RA Webb H.E., Bugarel M., Den Bakker H.C., Nightingale K., Granier S.A.,
RA Loneragan G.H.;
RT "Carbapenem-non-susceptible Bacteria Recovered from the Faeces of Dairy
RT Cattle.";
RL Submitted (SEP-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:KRW58770.1}.
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DR EMBL; LKKK01000012; KRW58770.1; -; Genomic_DNA.
DR RefSeq; WP_058068880.1; NZ_LKKK01000012.1.
DR AlphaFoldDB; A0A0T6UMI1; -.
DR STRING; 1729724.AO726_14720; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000051864; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000051864};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..524
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 534 AA; 57187 MW; 379414A21765E71B CRC64;
MTRCAQALVQ LLQAYDVDTV FGIPGVHTVE LYRALVDSGL RHISPRHEQG AGFMADGYAR
ASGKPGVCFI ITGPGMTNIL TAMGQAYADS IPMLVISTSL RREHQHLGHG HLHEMPDQRA
LVQGVCAFSH SLQCPTQLPE VLARAFAVFT CSRPRPVHIE IPLDVLMMSV AGLDLRPRHL
PRVPQPSAQD LAEAAKLLAR SQKPLILAGG GARHVGSVLD ELARQLCAPV ALSTNARGLL
PPEHPLLLDG VLSAPHGREL LDEADVVLAV GTELGETDYD FFGLGPLSFK GALIRLDIDP
QQVLGLHRAE VSLVGDATAG LQVLLPLIPA RTPLNGWGAG AVQRVNSCER QSWTPRQLVM
QGLLDCLRDT LPSPVLVGDS TQPVYQGAVG YRALQINGWF NAATGFGTLG YALPAAIGAK
LATPQQQVVA IIGDGGLQFS SAELLAAREA GVGLLIVLWN NQCYGEIRDY MQAQEVQPLG
VDILPPDFAA LAGAYGIHYH CLKSLPQLRQ LLPQLAGTDD VHLLELPAQD WLPD
//