ID K9AI56_9MICO Unreviewed; 543 AA.
AC K9AI56;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Thiamine pyrophosphate protein domain-containing protein TPP-binding protein {ECO:0000313|EMBL:EKU47008.1};
GN ORFNames=C272_09864 {ECO:0000313|EMBL:EKU47008.1};
OS Brevibacterium casei S18.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU47008.1, ECO:0000313|Proteomes:UP000009879};
RN [1] {ECO:0000313|EMBL:EKU47008.1, ECO:0000313|Proteomes:UP000009879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S18 {ECO:0000313|EMBL:EKU47008.1,
RC ECO:0000313|Proteomes:UP000009879};
RA Sharma R., Singh A., Jangir P.K.;
RT "Genome Sequence of Brevibacterium casei S18.";
RL Submitted (SEP-2012) 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:EKU47008.1}.
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DR EMBL; AMSP01000007; EKU47008.1; -; Genomic_DNA.
DR RefSeq; WP_009378464.1; NZ_AMSP01000007.1.
DR AlphaFoldDB; K9AI56; -.
DR PATRIC; fig|1229781.4.peg.1980; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000009879; 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; 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:UP000009879};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 543 AA; 55620 MW; A9A390193656032C CRC64;
MTELTGGGHL AKALAAEGVT RVFGIPGTHN LEVFAQLSAE GIDIVSPRHE QGAGYMADGA
ARTTGDVAVV VTTTGPAVLN ALTALLQSFT DSVPVLLIGP GMPLTHPGRG NGLLHEVRNQ
ALAIEAILGD SHRVTSVPEV SLAVGQALTV MRSGRPRPAF IEIPLDLIEA SGPGVLHPSV
TRPLPQVSVS AIESAAEALA DSQRPLLIVG AGAHGAGEEV IDLAETLGAG IVLSSNAKGA
VADDHPAVLG AIGFLPELPE ILGQADAVVA IGTELAPSDF WPQPLPLPGT VVRIDIDEMQ
MLRNAVVTHP IVADAREATA ALTAQAGRVR EAGSTDAARS WRVRLRDEAI AAADREGAPW
APLCEGLNAF TALSESPVVI AADSTMACYY GVQTGWRARR GDRFLYPAGA GTLGYGLPAG
IGAKIAAPES RVIAVEGDGG SMFTIAELSA AVQAQVSLTL VIVDNGGYGE IRNEMADRGD
VPSGVVLTAP DFPALATAMG AHGVHVESAE ELAAALAEAV ERPGPTLIHL FEDSRAAADM
LGP
//
