ID A0A0Q0T6A6_9PSED Unreviewed; 545 AA.
AC A0A0Q0T6A6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=5-guanidino-2-oxopentanoate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AQS70_00050 {ECO:0000313|EMBL:KQB55559.1};
OS Pseudomonas endophytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1563157 {ECO:0000313|EMBL:KQB55559.1, ECO:0000313|Proteomes:UP000050342};
RN [1] {ECO:0000313|EMBL:KQB55559.1, ECO:0000313|Proteomes:UP000050342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSTT44 {ECO:0000313|EMBL:KQB55559.1,
RC ECO:0000313|Proteomes:UP000050342};
RA Von Neubeck M., Huptas C., Wenning M., Scherer S.;
RT "Pseudomonas helleri sp. nov. and Pseudomonas weihenstephanensis sp. nov.,
RT isolated from raw cows milk.";
RL Submitted (OCT-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:KQB55559.1}.
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DR EMBL; LLWH01000001; KQB55559.1; -; Genomic_DNA.
DR RefSeq; WP_055100906.1; NZ_LLWH01000001.1.
DR AlphaFoldDB; A0A0Q0T6A6; -.
DR STRING; 1563157.AQS70_00050; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000050342; 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; 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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 57497 MW; 4F6A3CDDDEAD89CC CRC64;
MATCGEVLVK LLEAYGVEQV FGIPGVHTVE LYRGLARSSI HHVTPRHEQG AGFMADGYAR
TRGKPAVCFI ITGPGMTNIT TAMGQAYADS IPMLVISSVQ SRSQLGGGRG KLHELPDQRA
LVAGVAAFSH TLMSAAELPS VLARAFAVFQ AGRPRPVHIE IPLDVLVENA DALLSSQPVN
IARPGAAPAA IEQMSLRLIE AKRPLILAGG GAVDAAGALL QLAEHLGAPV ALTINAKGML
PSSHPLLIGS TQTLAATRAL VAEADVVLAI GTELAETDYD VTFAGGFEIP GALLRIDIDP
DQTVRNYPPT LALVADAQLA AEALLARLST QVLPERLADW GAERAGRLNM QLAATWDAPT
RAQTHFLQTV FEVLPQAVCV GDSTQPVYTG NLTFNPEHPR RWFNSSTGYG TLGYALPAAI
GAWLGRCVDG QPAGPVLCLI GDGGLQFTLP ELASAVEART PIIVLLWNNQ GYGEIKKYML
NRGIEPVGVD IYTPDLIGAA KALGCTALAV EGEAQLRAAL ASAVDRQGPT VIEIDEQHWQ
QTFAL
//
