ID   A0A2M9D8J0_9MICO        Unreviewed;       372 AA.
AC   A0A2M9D8J0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:PJJ82044.1};
GN   ORFNames=CLV85_1232 {ECO:0000313|EMBL:PJJ82044.1};
OS   Salinibacterium amurskyense.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Salinibacterium.
OX   NCBI_TaxID=205941 {ECO:0000313|EMBL:PJJ82044.1, ECO:0000313|Proteomes:UP000231742};
RN   [1] {ECO:0000313|EMBL:PJJ82044.1, ECO:0000313|Proteomes:UP000231742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16400 {ECO:0000313|EMBL:PJJ82044.1,
RC   ECO:0000313|Proteomes:UP000231742};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:PJJ82044.1}.
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DR   EMBL; PGFH01000001; PJJ82044.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9D8J0; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000231742; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:PJJ82044.1}.
FT   DOMAIN          57..324
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   372 AA;  40339 MW;  54FFA25F740364E9 CRC64;
     MSTTVPVKAQ MSGAKKQTPE FVQLLDPDGK RLSDELYDPW VSDVTGDQLA SLYEDLIIVR
     RIDTEATALQ RQGELGLWPP LFGQEAAQVG SARTLRPDDF VFSSYRENAV AYCRGVKLPD
     LLRVWRGTAS SGWDPFEVGM ATPAVIIGAQ TLHATGYAVG CTFDGVDSVS VAYFGDGATS
     EGDVNEAMVF AASFNAPVIF FCQNNQWAIS EPVGLQAQRP IADRAPGFGI PSIRVDGNDV
     LAVMAATRSA LDRARTGGGP TFIEAVTYRR GPHTTSDDPS RYVDPLVAKE WEARDPIARV
     EAFLRSEGVL TDELAASIQA RADEVAAEFR AGCLALENPE PLSVFDNVYA TEHSGLARQK
     SQYKAYLEGF DK
//