ID A0A418X8L1_9PSED Unreviewed; 541 AA.
AC A0A418X8L1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=5-guanidino-2-oxopentanoate decarboxylase {ECO:0000313|EMBL:RJG08817.1};
DE EC=4.1.1.75 {ECO:0000313|EMBL:RJG08817.1};
GN ORFNames=D3879_23435 {ECO:0000313|EMBL:RJG08817.1};
OS Pseudomonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320866 {ECO:0000313|EMBL:RJG08817.1, ECO:0000313|Proteomes:UP000284021};
RN [1] {ECO:0000313|EMBL:RJG08817.1, ECO:0000313|Proteomes:UP000284021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-6 {ECO:0000313|EMBL:RJG08817.1,
RC ECO:0000313|Proteomes:UP000284021};
RA Zhu H.;
RL Submitted (SEP-2018) 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:RJG08817.1}.
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DR EMBL; QYUR01000008; RJG08817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418X8L1; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000284021; Unassembled WGS sequence.
DR GO; GO:0047435; F:5-guanidino-2-oxopentanoate decarboxylase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:RJG08817.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 541 AA; 57846 MW; 5B832917AA2BE993 CRC64;
MTTCAQSLVH LLEGYGVKTI FGIPGVHTVE LYRGLHGSSL THMSPRHEQG AGFMADGYAR
ASGNPAVCFI ITGPGMTNIL TAMGQAYADS VPMLVISTTN RREQLRLGHG HLHELPDQRA
MIAGVCAFSH TLQSPAELPE LLARAFGIFN CARPRPVHIE IPLDVLEMSA DSLDLLPRTL
PNPPAPAPAA IKEAAKLLDT AKRPLILAGG GARRAAEALQ QLAERLQAPV ALTTNARGLL
PCGHPLLLDG VQSSAHGRAL FDEADVVLAV GTELGETDYD FFGLGPVQFQ APLIRLDIDP
MQVMGAQRAQ VGLVGDANEG LQALLAQTTP NHPRGSWAVD SVVRVNNCER ASWTAKQNSL
QALLDLLRDT LKNPLIVGDS TQPVYQGALG YQAPQANSWF NAGTGYGTLG YGLPAAIGAK
LALPQRPVVA LVGDGGMQFS CAELIAAREA GIGVILLLWN NQCYAEIRDY MEAREIPPLG
VNILPPDFEA MARSFHVAHH APQSPESLRA LLLELAETTQ PVMIELDAAT LLPQLNRKYV
E
//
