ID A0A161SRH9_9MICO Unreviewed; 538 AA.
AC A0A161SRH9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative 2-ketoarginine decarboxylase AruI {ECO:0000313|EMBL:KZE94685.1};
GN Name=aruI {ECO:0000313|EMBL:KZE94685.1};
GN ORFNames=AVP42_00612 {ECO:0000313|EMBL:KZE94685.1};
OS Agromyces sp. NDB4Y10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1775951 {ECO:0000313|EMBL:KZE94685.1, ECO:0000313|Proteomes:UP000185889};
RN [1] {ECO:0000313|EMBL:KZE94685.1, ECO:0000313|Proteomes:UP000185889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NDB4Y10 {ECO:0000313|EMBL:KZE94685.1,
RC ECO:0000313|Proteomes:UP000185889};
RA Adelskov J., Patel B.K.;
RT "Draft genome sequence of Agromyces sp. NDB4Y10 isolated from a newly
RT drilled coal seam bore well.";
RL Submitted (JAN-2016) 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:KZE94685.1}.
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DR EMBL; LQGY01000014; KZE94685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161SRH9; -.
DR STRING; 1775951.AVP42_00612; -.
DR PATRIC; fig|1775951.3.peg.634; -.
DR Proteomes; UP000185889; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000185889};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 17..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 207..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 538 AA; 55734 MW; B22BBAB8D57831A0 CRC64;
MTMTQTPVDL AAPYADTAGR AVLETIRAYG VTTIFGIPGT HNLELYRPLA DLGIRAVTNR
HEQGAGYGAD GWAQQTGLPG VVITTSGPGL QNAMSAIGTA FCESRPLIVL SPGVALGEEF
RDVGTLHETK DASAMVAAIA EWSRRVTSAA EAVDAVHDAF ELFRTGRPRP VHIEIPLDVL
ESPAEVPAAA RMARPAPPSD RGEAGLIREA AELLASAASP VIIAGGGATR ATAEVTALAE
RLGAPVLTTL NGKGTVDERH PLALGSNLRL AAARAVAEAA DVLVVLGSKL GEAELWAPSL
RAGGRVIRID RSVAQLDKNL EATVGIVGDC AAVTAELVAA LPVSERPSPD LSTARRAIAD
EIRSTAPDTV ALAEQIAEAL PDDVIVAGDS SQIIYLALAN VLECSSPHSL LYTPTYATLG
YGLPAAIGAK VARADRPVVA VLGDGALMFA VNELATAVEQ RLDVTIVCVD NGGYAEIRQN
EVDRGIRPIG VELVQPDWAA LADAFGATGR PVSDRAELGS AIRSAIADGG VQLVHIRQ
//
