ID A0A1L9QT89_9CYAN Unreviewed; 655 AA.
AC A0A1L9QT89;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:OJJ25859.1};
GN ORFNames=BI308_08975 {ECO:0000313|EMBL:OJJ25859.1};
OS Roseofilum reptotaenium AO1-A.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Desertifilales; Desertifilaceae;
OC Roseofilum.
OX NCBI_TaxID=1925591 {ECO:0000313|EMBL:OJJ25859.1, ECO:0000313|Proteomes:UP000183940};
RN [1] {ECO:0000313|EMBL:OJJ25859.1, ECO:0000313|Proteomes:UP000183940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-A {ECO:0000313|EMBL:OJJ25859.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:OJJ25859.1}.
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; MLAW01000012; OJJ25859.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9QT89; -.
DR STRING; 1925591.BI308_08975; -.
DR Proteomes; UP000183940; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24321; DEHYDROGENASES, SHORT CHAIN; 1.
DR PANTHER; PTHR24321:SF14; SHORT-CHAIN TYPE DEHYDROGENASE_REDUCTASE BLR2146-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000183940}.
FT DOMAIN 20..221
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 655 AA; 71389 MW; D2AC25178807E9A5 CRC64;
MVKNLWNQSE AAQYTTDLEQ RVYTSRLLGK DPSLVLHGGG NTSVKVKETN LFGEKEDILY
VKGSGWDLAT IEAEGFAPVR IPHLLKLAQL EQLSDPQMVN ELKTQMTRAS APYPSVETIL
HAILPYKYVD HTHADAIIAV TNTANGRKRV EEIYGDRLIV IPYVMPGFDL ARVCARQFAL
EAGEHALGMV LMNHGIFSFG ATAQESYERM IELVSQAESY LQKQGAITSI PEQPVPEPAP
LSHTLAQLRH TLSKTTQFPV ILSTHRNPKT LSFAQREDIQ HISQQGPATP DHVIRTKRLP
LVGRDIQSYV EAYQAYFRAH ATPDLTILDP IPRVILDPEL GMCTVGKTVK QAHIVADIYD
HTIDIISTST QLGGYQALSA KDIFAVEYWD LEQAKLRKGG KPPLFTGEIA LVTGAASGIG
KACVDSLLKR GAAVIGLDID TKIESLYNRA DFYGITCDVT DETALIAAPE QAVQRFGGLD
MLILNAGIFP GGCPIADLDT SEWRKVMSVN LDANLALLRH AYPLLKLAPQ GGRVVVIGSK
NVPAPGPGAA AYSASKAALN QLMRVAALEW GKDNIRLNSL HPNAVFDTGL WTEDVLNARA
AHYGLIVEEY KTNNVLKVEV DSHSVAELAA EMCGPLFAKT TAAQVPVDGG NDRVI
//
