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Database: UniProt
Entry: A0A0B0DFJ5_9MICC
LinkDB: A0A0B0DFJ5_9MICC
Original site: A0A0B0DFJ5_9MICC 
ID   A0A0B0DFJ5_9MICC        Unreviewed;       305 AA.
AC   A0A0B0DFJ5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Shikimate dehydrogenase {ECO:0000313|EMBL:KHE74917.1};
GN   ORFNames=AS25_03720 {ECO:0000313|EMBL:KHE74917.1};
OS   Kocuria marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=223184 {ECO:0000313|EMBL:KHE74917.1, ECO:0000313|Proteomes:UP000030664};
RN   [1] {ECO:0000313|EMBL:KHE74917.1, ECO:0000313|Proteomes:UP000030664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO9-6 {ECO:0000313|EMBL:KHE74917.1,
RC   ECO:0000313|Proteomes:UP000030664};
RA   Castro D.B., Pereira L.B., Silva M.V., Silva B.P., Zanardi B.R., Carlos C.,
RA   Belgini D.R., Limache E.G., Lacerda G.V., Nery M.B., Gomes M.B., Souza S.,
RA   Silva T.M., Rodrigues V.D., Paulino L.C., Vicentini R., Ferraz L.F.,
RA   Ottoboni L.M.;
RT   "High-quality draft genome sequence of Kocuria marina SO9-6, an
RT   actinobacterium isolated from a copper mine.";
RL   Submitted (SEP-2014) 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:KHE74917.1}.
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DR   EMBL; JROM01000016; KHE74917.1; -; Genomic_DNA.
DR   RefSeq; WP_035961747.1; NZ_JROM01000016.1.
DR   AlphaFoldDB; A0A0B0DFJ5; -.
DR   STRING; 223184.AS25_03720; -.
DR   eggNOG; COG0169; Bacteria.
DR   Proteomes; UP000030664; Unassembled WGS sequence.
DR   GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR013708; Shikimate_DH-bd_N.
DR   InterPro; IPR022893; Shikimate_DH_fam.
DR   PANTHER; PTHR21089:SF1; BIFUNCTIONAL 3-DEHYDROQUINATE DEHYDRATASE_SHIKIMATE DEHYDROGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR21089; SHIKIMATE DEHYDROGENASE; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF08501; Shikimate_dh_N; 1.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
FT   DOMAIN          10..93
FT                   /note="Shikimate dehydrogenase substrate binding N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08501"
FT   DOMAIN          114..201
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01262"
SQ   SEQUENCE   305 AA;  31853 MW;  D1B8B5E42B0433B7 CRC64;
     MTRSSVRAAV LGHPVDHSLS PVLHAAAYEA LGLTAHYTRR DVPVGEWDTF WAGARAAGDW
     GGFSVTMPLK PLAARDADRV TPLVRALGVA NTLTFEDDGR VVADNTDVMG IMSAVSAAGA
     IPGTPRAVVL GGGATASAAV AALHGLGAET VDVVVRTPSR ARTLEAVARA VGTEVRTVAW
     EHAAEALHTA DVVVATLPPR GADELALQWR AQAPSVSGVL LDAAYDPWPS RLASAWQDAG
     GAIAPGVDML IFQAVDQVRW FTQGDPRAAV PHEDRVTAAM CRAVGRPERG IPQRVRTAQA
     TRLAP
//
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