ID X1HI67_9ZZZZ Unreviewed; 111 AA.
AC X1HI67;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=KARI C-terminal knotted domain-containing protein {ECO:0000259|PROSITE:PS51851};
DE Flags: Fragment;
GN ORFNames=S03H2_14608 {ECO:0000313|EMBL:GAH44968.1};
OS marine sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAH44968.1};
RN [1] {ECO:0000313|EMBL:GAH44968.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAH44968.1};
RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA Takami H.;
RT "High frequency of phylogenetically diverse reductive dehalogenase-
RT homologous genes in deep subseafloor sedimentary metagenomes.";
RL Front. Microbiol. 5:80-80(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004885}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318}.
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:GAH44968.1}.
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; BARU01007416; GAH44968.1; -; Genomic_DNA.
DR AlphaFoldDB; X1HI67; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013023; KARI.
DR InterPro; IPR000506; KARI_C.
DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01450; IlvC; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR PROSITE; PS51851; KARI_C; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..106
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAH44968.1"
SQ SEQUENCE 111 AA; 12910 MW; 82007DEDC0252E19 CRC64;
SAIFEVLSEL KLIVDLIYEG GISWMRYSIS DTAEYGDMVK GKKVITSETR KNMKKILKDI
QSGAFAREWI LENKAGRPVY NAIKKKEENH LIEKVGKELR KMMTWIKKEE D
//
