ID G7ZIK8_AZOL4 Unreviewed; 356 AA.
AC G7ZIK8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN OrderedLocusNames=AZOLI_p60039 {ECO:0000313|EMBL:CBS91462.1};
OS Azospirillum lipoferum (strain 4B).
OG Plasmid AZO_p6 {ECO:0000313|EMBL:CBS91462.1,
OG ECO:0000313|Proteomes:UP000005667}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS91462.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC PLASMID=Plasmid AZO_p6 {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ311874; CBS91462.1; -; Genomic_DNA.
DR RefSeq; WP_014189889.1; NC_016588.1.
DR AlphaFoldDB; G7ZIK8; -.
DR KEGG; ali:AZOLI_p60039; -.
DR HOGENOM; CLU_012907_1_0_5; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000005667; Plasmid AZO_p6.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CBS91462.1};
KW Plasmid {ECO:0000313|EMBL:CBS91462.1};
KW Pyruvate {ECO:0000313|EMBL:CBS91462.1}.
FT DOMAIN 11..186
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 356 AA; 38776 MW; 6DBAD11C27AB50A5 CRC64;
MSSPNAATRQ LRYVDALAEA VSQEMARDES VFVFGLDVDD HKAIQGSTRG LLERFGPERI
FTTPLSEDAM TGVAIGAAMA GMRPIHVHIR MDFLLLCMNQ LVNMAAKAHY MYGGAVKVPM
VARSMIGKSW GQGAQHSQGL HSMFMHVPGL KVVAPSNAYD AKGCMIAAIR DDNPVIFMEH
RLLYPTEAPV PEAPYTVEFG RARRMLEGGD ITVVGVSNMA IECLRAAELL REVDVGVDLI
DPITLVPLDI DTIVDSVART RRLLVVDNSW INCGASAEIA SQVSERLGGS GPLQIRRMGF
APTTCPTTPA LEQHFYPNPS TIAEAAYAMA RPNGSPWRPD PEHARLAYQA QFKGPF
//
