ID A0A516GD09_9MICO Unreviewed; 381 AA.
AC A0A516GD09;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=Bifunctional chorismate mutase/prephenate dehydrogenase {ECO:0000313|EMBL:QDO89401.1};
DE EC=1.3.1.12 {ECO:0000313|EMBL:QDO89401.1};
DE EC=5.4.99.5 {ECO:0000313|EMBL:QDO89401.1};
GN Name=tyrA {ECO:0000313|EMBL:QDO89401.1};
GN ORFNames=FNH13_14570 {ECO:0000313|EMBL:QDO89401.1};
OS Ornithinimicrobium ciconiae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=2594265 {ECO:0000313|EMBL:QDO89401.1, ECO:0000313|Proteomes:UP000315395};
RN [1] {ECO:0000313|EMBL:QDO89401.1, ECO:0000313|Proteomes:UP000315395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H23M54 {ECO:0000313|EMBL:QDO89401.1,
RC ECO:0000313|Proteomes:UP000315395};
RA Bae J.-W., Lee S.-Y.;
RT "complete genome sequencing of Ornithinimicrobium sp. H23M54.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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; CP041616; QDO89401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A516GD09; -.
DR KEGG; orz:FNH13_14570; -.
DR OrthoDB; 3267837at2; -.
DR Proteomes; UP000315395; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 1.20.59.10; Chorismate mutase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR008244; Chor_mut/prephenate_DH_T.
DR InterPro; IPR036263; Chorismate_II_sf.
DR InterPro; IPR036979; CM_dom_sf.
DR InterPro; IPR002701; CM_II_prokaryot.
DR InterPro; IPR011277; CM_T.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR NCBIfam; TIGR01799; CM_T; 1.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01817; CM_2; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR PIRSF; PIRSF001499; Chor_mut_pdh_Tpr; 1.
DR SMART; SM00830; CM_2; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF48600; Chorismate mutase II; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51168; CHORISMATE_MUT_2; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:QDO89401.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:QDO89401.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000315395}.
FT DOMAIN 8..99
FT /note="Chorismate mutase"
FT /evidence="ECO:0000259|PROSITE:PS51168"
FT DOMAIN 108..370
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 381 AA; 42914 MW; 87FBEFCE89F0E58B CRC64;
MEQPHPSAGP EAPLAELRDQ IDAVDKQVMD LLARRLELVA EVGELKGQHG LPIYAPERER
TMIAARRTEA ERRGLPPDLI EDVLRRCMRE AYAHEKNLGF TRQSPDLGPI VIVGGAGQMG
QLFGRMLRLS GYEVRELDRD DWDNSQQLFD GVGMVLVSVP IHDTVSVIHQ LPPLPADCLL
VDLTSTKLAP MEAMLQVHEG PVLGLHPMFA PDVDNLAKQV IAYVPGRHPD ASTWLLEQIR
LWGARLHEVS AQDHDHAMGL IQAQRHFSTF AYGLHLIRED RSLDELLALS SPIYRLELIM
IGRLFAQDPE LYADIILSSP DHLELLDRYH ERFAEALEIL RAGDREAFIA RFREIGAWFG
PSAERFMAES RTLLAHADAQ R
//