ID M4Z6F4_9BRAD Unreviewed; 577 AA.
AC M4Z6F4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Putative oxalyl-CoA decarboxylase with thiamin thiamine pyrophosphate (TPP) domain {ECO:0000313|EMBL:BAM88752.1};
GN ORFNames=S58_27460 {ECO:0000313|EMBL:BAM88752.1};
OS Bradyrhizobium oligotrophicum S58.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM88752.1, ECO:0000313|Proteomes:UP000011841};
RN [1] {ECO:0000313|EMBL:BAM88752.1, ECO:0000313|Proteomes:UP000011841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S58 {ECO:0000313|EMBL:BAM88752.1,
RC ECO:0000313|Proteomes:UP000011841};
RX PubMed=23396330; DOI=10.1128/AEM.00009-13;
RA Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A.,
RA Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T.,
RA Minamisawa K.;
RT "Genome analysis suggests that the soil oligotrophic bacterium Agromonas
RT oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont
RT of Aeschynomene indica.";
RL Appl. Environ. Microbiol. 79:2542-2551(2013).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AP012603; BAM88752.1; -; Genomic_DNA.
DR RefSeq; WP_015665874.1; NC_020453.1.
DR AlphaFoldDB; M4Z6F4; -.
DR STRING; 1245469.S58_27460; -.
DR KEGG; aol:S58_27460; -.
DR PATRIC; fig|1245469.3.peg.2824; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_3_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000011841; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008949; F:oxalyl-CoA decarboxylase activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0033611; P:oxalate catabolic process; IEA:InterPro.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR045025; HACL1-like.
DR InterPro; IPR017660; Oxalyl-CoA_decarboxylase.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR03254; oxalate_oxc; 1.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 20..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 211..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..550
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 577 AA; 61207 MW; A6067565131E4707 CRC64;
MAQTAIKTEA PDTQQELTDG FHLVIDAMKL NGIDTIYNVP GIPITDLGRM AQAEGIRVLS
FRHEQNAGYA AAIAGFLTKK PGVCLTVSAP GFLNGLTALA HATTNCFPMI LVSGSSEREI
VDLQQGDYEE MDQLAIAKPL CKAAFRVLHA QDIGIGFARA IRAAVSGRPG GVYLDLPAKL
FGQVMNAQAG AASLVKVIDP SPAQIPSPDS VKRALDVLKS AKRPLIILGK GAAYAQADEA
IKNFVEKSGV PFLPMSMAKG LLPDLHPQCA GAARSTVLKD SDVVMLIGAR LNWLLSHGKG
KSWGDAPKKF IQVDIEPKEM DSNVEIAAPV VGDIGSVVTA FSEAMGSNWT KAPVEWLSAV
QKKREDNVAK MAPRLMNNNS PMDYHGALGV LRTIIKERPD AILVNEGANT LDLARGVIDM
YQPRKRLDVG TWGVMGIGMG SAIAAAVETG KPVLAIEGDS AFGFSGMEVE TICRYNLPIC
VVIFNNDGIY RGTDQNSAGD DPATTVFVKG ARYDKMMEAF GGVGVNATSP DELKRAVNEA
MDSGKPTLIN AVIDPAAGSE SGRIGNLNPQ SVLTKKK
//
