ID A0A0P1INC3_9RHOB Unreviewed; 540 AA.
AC A0A0P1INC3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative 2-ketoarginine decarboxylase AruI {ECO:0000313|EMBL:CUJ86447.1};
DE EC=4.1.1.75 {ECO:0000313|EMBL:CUJ86447.1};
GN Name=aruI {ECO:0000313|EMBL:CUJ86447.1};
GN ORFNames=PH7735_00621 {ECO:0000313|EMBL:CUJ86447.1};
OS Shimia thalassica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUJ86447.1, ECO:0000313|Proteomes:UP000051870};
RN [1] {ECO:0000313|Proteomes:UP000051870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA Rodrigo-Torres Lidia, Arahal R.David.;
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}.
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DR EMBL; CYTW01000001; CUJ86447.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1INC3; -.
DR STRING; 1715693.PH7735_00621; -.
DR Proteomes; UP000051870; 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 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 Lyase {ECO:0000313|EMBL:CUJ86447.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051870};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 16..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 540 AA; 57743 MW; ADC1BE3E9BC57DF1 CRC64;
MTSTTAEQDG AVRPLGAQIS HMLKQRGVDT IFGIPGVHNV EMYRGIEEAG IQHVLARHEQ
GAGFMADGYA RATGGFGVCY VITGPGLLNT LTPLGQAYSD SVAVLAISSC LDETAARRGQ
LHQMLDQEAA ADTVCDWSHE AKSPEAAYTL VDRALTEFAA QRKRPKHMQV PIARLGAMAP
QAPVAVGAKQ TAGRRTPGDL SSFAATVLAA QKPLFIFGGG VGRHGNEETV RAAMHRCGAA
AFTTYAGGGL LEADDPMSFG CYLGRPESER FIAESDLVIA IGTELSECDL WRNELGHTGT
FVRVDIDPEV LSDEHRADIV FHADGIAFLG ELLSHFPDET PAKWDADQIS AAKARFKAET
DAERPGIVEI CDALASVMPE DAMVYSDMTQ FAYVAKEVWN MPRAGHWHHP SGFGTLGYAL
PASIGGAVAR AGLPTVCIAG DYGFQYTIQE FGTAVELGLP LPILLWDNGK LKEIEDSMVA
SQIAPNAVIA QNPDFCKLAE AYGAHAKAPK TLDELQAALL EAFKADRPTL IHMTPELTAK
//
