ID A0A1F1KEX7_9MICO Unreviewed; 334 AA.
AC A0A1F1KEX7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=KARI N-terminal Rossmann domain-containing protein {ECO:0000259|Pfam:PF07991};
GN ORFNames=HMPREF3099_04905 {ECO:0000313|EMBL:OFS14102.1};
OS Kytococcus sp. HMSC28H12.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC Kytococcus.
OX NCBI_TaxID=1581067 {ECO:0000313|EMBL:OFS14102.1, ECO:0000313|Proteomes:UP000176675};
RN [1] {ECO:0000313|EMBL:OFS14102.1, ECO:0000313|Proteomes:UP000176675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC28H12 {ECO:0000313|EMBL:OFS14102.1,
RC ECO:0000313|Proteomes:UP000176675};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OFS14102.1}.
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DR EMBL; LWPN01000142; OFS14102.1; -; Genomic_DNA.
DR RefSeq; WP_070704748.1; NZ_KV824390.1.
DR AlphaFoldDB; A0A1F1KEX7; -.
DR Proteomes; UP000176675; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013023; KARI.
DR InterPro; IPR013116; KARI_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF07991; IlvN; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000176675}.
FT DOMAIN 38..184
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|Pfam:PF07991"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 34298 MW; 0F0F50725FA44DC3 CRC64;
MNAPQQPGTP AHDAAHADAT RPGSTAWWGP WDADRSVVAD REVAVIGFDA TAELHAQNLR
DSGVDVRVGA EPGTPEHDAA QAEGFFTLPV ADAVQDGELV VIGTAHLEAV AAVLTDEQVL
VLTSAAAGRA LRGSGIRHRG VILLVEVLGE PVATRQAYVD GRGGPAVVAV VARGTGSGHE
LTLTLNPTAA PAAPDARGDA AQRLAVAYAD VVGATRAAAI GVDALDWAVA ADFADTRVTP
LLEAVLAAGR DALVAQGFDP VVADLAVLHR LQSTWEALGH EGARPSAADE HREEVARLTG
PAPRSRSRRT APVDDDATAA ARHARLGEAF GGAR
//
