ID A0A1E7JYZ2_9ACTN Unreviewed; 775 AA.
AC A0A1E7JYZ2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 05-FEB-2025, entry version 27.
DE SubName: Full=2-dehydropantoate 2-reductase {ECO:0000313|EMBL:OEU96882.1};
GN ORFNames=AN216_18165 {ECO:0000313|EMBL:OEU96882.1};
OS Streptomyces oceani.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1075402 {ECO:0000313|EMBL:OEU96882.1, ECO:0000313|Proteomes:UP000176101};
RN [1] {ECO:0000313|EMBL:OEU96882.1, ECO:0000313|Proteomes:UP000176101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 02100 {ECO:0000313|EMBL:OEU96882.1,
RC ECO:0000313|Proteomes:UP000176101};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:OEU96882.1}.
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DR EMBL; LJGU01000133; OEU96882.1; -; Genomic_DNA.
DR RefSeq; WP_070197731.1; NZ_LJGU01000133.1.
DR AlphaFoldDB; A0A1E7JYZ2; -.
DR STRING; 1075402.AN216_18165; -.
DR PATRIC; fig|1075402.3.peg.4793; -.
DR OrthoDB; 9783294at2; -.
DR Proteomes; UP000176101; Unassembled WGS sequence.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR003710; ApbA.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR050072; Peptidase_M20A.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000176101}.
FT DOMAIN 14..158
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 186..326
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT DOMAIN 577..669
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 437..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 81840 MW; D7D4C7212C156FBB CRC64;
MTHLSTDPHT RPYTVVGAGA IGGTLAYALA SAGHPVTVVD TDREHVEAIR THGLVREKDG
VRERITLKAT TPEECTGPLR RVLLAVKAQA TERALDWLAP RLVPDGYVVS VQNGFNEPLI
AERVGGDRTL AAFVNIFADV IEPGVIRDGG HGALVVGQPG GGVIGARVRD LVTDLRAWGP
AQASDNVEGY LWAKAGFGAM LAATALADDT MADLIDRHRP AMYALAAEVF DVAATTGTRL
EPFDAFEAHA FTREADPAVR DAACDRLTAW LRGQPKNRSG IWRDLAVRRR PVEVTTHYAS
VFETADRAGL DTPVLRRVVT ALRELEDDPG GMSEERLADL DRIASGDVRE LPGVPALTDE
QAGAVQDWLR DRHEEMVADL AAYTERGSSS EDPEALRSCL SWLRDWLGAS LGPPEKEELL
RREGGRDILV QRYPGVRDAR TGGHSSRDGA GRAGGADTAG GADTAGGADT AEQPVLLLCH
YDTVWPTGTL LDWPFRREGD RVSGPGVFDM KAGLVQAVWA LRALDALRLP RPPCTLLLNG
DEETGSHASS ETILAEARTS RAALVFEASA EGAVKTTRKG VGLFTLVVTG TEAHAGLDPE
AGASAVDELA QQVLRLRALD DPAAGTSVNV GVVHGGTRSN VTAGRAVAEL DVRVASRAEQ
KRVDAALDEL TPVDERTSLG VSGGWNRPVF ERTRDVARMY QLARACAAPL GLDLREAAVG
GASDGNFVLA AGTPVLDGIG AVGAGAHARS EHATVSGMTE RSALAAGVLA ALAIG
//
