ID A0A1H4Z6I2_9PSEU Unreviewed; 301 AA.
AC A0A1H4Z6I2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Ketoreductase RED1 {ECO:0000313|EMBL:SED25537.1};
GN ORFNames=SAMN04489727_7106 {ECO:0000313|EMBL:SED25537.1};
OS Amycolatopsis tolypomycina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=208445 {ECO:0000313|EMBL:SED25537.1, ECO:0000313|Proteomes:UP000199622};
RN [1] {ECO:0000313|EMBL:SED25537.1, ECO:0000313|Proteomes:UP000199622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44544 {ECO:0000313|EMBL:SED25537.1,
RC ECO:0000313|Proteomes:UP000199622};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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DR EMBL; FNSO01000004; SED25537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4Z6I2; -.
DR STRING; 208445.SAMN04489727_7106; -.
DR OrthoDB; 9771883at2; -.
DR Proteomes; UP000199622; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..174
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 178..248
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT SITE 131
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 301 AA; 32304 MW; 18C4611146079E85 CRC64;
MKNAAVIGAG TIGLSWTALF AHHGLTVRVT DPRPDLADAV SQALAQFAPH LGTTADELAS
RVQIAADVTE AVRDADVVQE NGPENVEFKK DLFKQLVDEA PAHALQLSSS SAIPSTAFTG
EIDGSRVLIG HPFNPPHLIP LVEVVPGERT SDEAVQQAVD FYTSLGRTPV VERKEIPGFV
GNRLQNALSR EAIYLVEQGV VTPEDLDKVI TNSLGIRWAT VGPFLGSHLG GGLGGYRHMA
EHIGKSMKQM WAGLGNPSQS PEEQEQLIEA VEKAYGSSTY SELAETRDRK QLAVLSALEE
N
//
