ID A0A148KMU3_9ALTE Unreviewed; 730 AA.
AC A0A148KMU3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:KXI27565.1};
GN ORFNames=AX660_01020 {ECO:0000313|EMBL:KXI27565.1};
OS Paraglaciecola hydrolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1799789 {ECO:0000313|EMBL:KXI27565.1, ECO:0000313|Proteomes:UP000070299};
RN [1] {ECO:0000313|EMBL:KXI27565.1, ECO:0000313|Proteomes:UP000070299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S66 {ECO:0000313|EMBL:KXI27565.1,
RC ECO:0000313|Proteomes:UP000070299};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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:KXI27565.1}.
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DR EMBL; LSNE01000010; KXI27565.1; -; Genomic_DNA.
DR RefSeq; WP_068380152.1; NZ_LSNE01000010.1.
DR AlphaFoldDB; A0A148KMU3; -.
DR STRING; 1799789.AX660_01020; -.
DR OrthoDB; 9774430at2; -.
DR Proteomes; UP000070299; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005996; P:monosaccharide metabolic process; IEA:UniProt.
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; IPR013454; Bifunc_RhaD/ADH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR02632; RhaD_aldol-ADH; 1.
DR PANTHER; PTHR43008; BENZIL REDUCTASE; 1.
DR PANTHER; PTHR43008:SF4; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR PRINTS; PR00081; GDHRDH.
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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070299}.
FT DOMAIN 28..237
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 730 AA; 79817 MW; F70A7C0B7D8D1B26 CRC64;
MGYRPVEYKH VNYLWEDDVA DKLDPVDNLV YRSNVLGADQ RITNTGGGNT SAKLMESDPL
TGEQVEVLWV KGSGGDLRTS NKDNFSSLYS GKLQALDTFY QQQPEKGYKS AGEDTMVGMF
KHCNFCLNPR ASSIDTPLHS MIAEKHIDHL HPNAVIAIAS CKDQEALTAK VWQGKLAYVP
WMRPGWEAAK VCEDTYAKNP DIDGILLGQH GHTNWASESK SCYETSLWVI ETAARYIEQH
DKGDKTFGGQ QHQSLGSDDV TALLYQFLPT ARGLLSDKVK FVATVQSDAT TLRFVNSFDA
KRLSDLGTSC PDHFLRTKIK PLFVDFDPLK DDLATLVSKF KAGLAQYRID YTAYYEQCKR
PDSPPMRDPS PTVILIPGVG LIAWGKNKSE SRVTAEFYNC AIEVMRGAEA ISEYTALPVQ
EAFDIEYWAL EEAKLQRMPA EKTLARNVVV VIGAGDGIGK ATAHRVAAEG AHVVCADLRL
EAAQVTAAEL TKKYGQGIGV AGTGISNCGP AIALSVDITK RNSVQNMFEQ VVLAYGGIDN
VIVTAGVFMA EGEDYDRNDE IFDFSFAVNV KGGYVVGSEA NKIWQRQNIK GSMVLTTSVN
AAVSKKGSLA YDTSKAAANH LVRELAVSFA PLVNVNALAP ATVVQGSTMF PRDRVISSLS
KYNIAFNESE ETDSLRTKLA EFYAQRTLTK QPITPADQAE AAYLLISGQL SKTTGQVISV
DGGLHEAFLR
//
