ID Q98CC6_RHILO Unreviewed; 526 AA.
AC Q98CC6;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Acetohydroxy acid synthase {ECO:0000313|EMBL:BAB51695.1};
GN OrderedLocusNames=mlr5207 {ECO:0000313|EMBL:BAB51695.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB51695.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB51695.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; BA000012; BAB51695.1; -; Genomic_DNA.
DR RefSeq; WP_010913034.1; NC_002678.2.
DR AlphaFoldDB; Q98CC6; -.
DR KEGG; mlo:mlr5207; -.
DR PATRIC; fig|266835.9.peg.4122; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR Proteomes; UP000000552; Chromosome.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 526 AA; 54307 MW; E80199A0C31FECAF CRC64;
MTTLGEALIT LLEAHGVDTV FGIPGVHTVE LYRGLARSKI RHVTPRHEQG AGFMADGYAR
ASGRPGVAFV ITGPGLTNTI TAMGQARADS VPMLVISGVN ATPTLGKGLG FLHELPDQRG
MMEKVALLSR RVTEASELPD ALAQAFALFS SSRPGPVHIE IPTDVMVKPA DDIAALLSNA
APPTPDGAAI ASAAKLITAA RRPLILAGGG AKRAEMALRR LAETLGAPVV ETTNARGLLH
RHPLCVPASP SLKAVRALMA EADLVIAAGT EFGPTDYDGY GDGGFVLPSN LIRIDIGADQ
LARRPVTVGI QADCAEAIEA LLAAIGTAHP AAPDGEARAT AARKAAFAEL SPAYLAQVHA
VEMIRDALPG AIVVGDSTQP VYAANLYYDH DRPGGWFNAA TGFGALGYGP PAAIGAALAV
PDAPVVCLTG DGGFQFTLPE LGAALDAKAP VIFVVWNNRG YREIETSMLD VGVEPVGVSP
APPDFCKLAE AYGIGAERLA DIGALPQALK RARATGLPCV IEITVD
//
