ID A6FI15_9GAMM Unreviewed; 665 AA.
AC A6FI15;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Short chain dehydrogenase {ECO:0000313|EMBL:EDM65219.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:EDM65219.1};
GN ORFNames=PE36_17952 {ECO:0000313|EMBL:EDM65219.1};
OS Moritella sp. PE36.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM65219.1, ECO:0000313|Proteomes:UP000004278};
RN [1] {ECO:0000313|EMBL:EDM65219.1, ECO:0000313|Proteomes:UP000004278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE36 {ECO:0000313|EMBL:EDM65219.1,
RC ECO:0000313|Proteomes:UP000004278};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM65219.1}.
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DR EMBL; ABCQ01000060; EDM65219.1; -; Genomic_DNA.
DR RefSeq; WP_006034022.1; NZ_ABCQ01000060.1.
DR AlphaFoldDB; A6FI15; -.
DR STRING; 58051.PE36_17952; -.
DR OrthoDB; 9810734at2; -.
DR Proteomes; UP000004278; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd05263; MupV_like_SDR_e; 1.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR44196; DEHYDROGENASE/REDUCTASE SDR FAMILY MEMBER 7B; 1.
DR PANTHER; PTHR44196:SF5; POSSIBLE MULTI-FUNCTIONAL ENZYME WITH ACYL-COA-REDUCTASE ACTIVITY ACRA1; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EDM65219.1}.
FT DOMAIN 5..236
FT /note="Thioester reductase (TE)"
FT /evidence="ECO:0000259|Pfam:PF07993"
SQ SEQUENCE 665 AA; 74039 MW; 46E288637AA9DBDA CRC64;
MKYLVTGGTG FIGRFLIERL VEREDAQVYV LTRQGSEHKF NALKDRVHKS VKSRIKMVTG
DITKVNLGID ELWLAEHTDQ IDNVYHLAAI YDMKADAESQ ETANIVGTRN AVEASVKIKA
KSFHHVSSIA AAGLFNGTFY EDMFEEAENM DNAYLRTKHI SEKVVRDECS IPFRIYRPGM
VVGHSKTGEI DKVDGPYYFF KLLKKIRETI PTWMPMIGVE GRRLNIVPVD YVADAIDYIS
HKEDVHSNCF HLVDPKPFKV GEVLNIFATA GNAPRTAFRI DSRIANFLPA SVRQAITHLP
AVKQLTEGVL NDLGIPKDVL NFLNYPTTFD DRETARALEG SNIKVPRLDE YAPAVWDYWE
RNLNDDLIND MTLKGNVSGK TIVITGASSG IGEATALKLA PTGAKLILVA RDVTKLEATQ
AQIQELGGDA HIYSCDISNM ESCDELVKSV LAEHGFVDIL INNAGRSIRR SIDLSFDRFH
DYERTMQLNY FGSIRLIMGF TPSMLEHKKG HVINISSIGV LTNSPRFSAY VASKAALDAF
TRCAASEFSD RNVNMTTINM PLVRTPMIGP TKVYDNVPTL APSEAADLIV QAIIRKPKRI
ATKIGIMSEV LYSLFPKVSE IIMNTGYRMF NDSAAAKGKE EDKDAPTQAS TEQVAFAAIM
RGVHW
//
