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Database: UniProt
Entry: A0A1V3SGU4_9BURK
LinkDB: A0A1V3SGU4_9BURK
Original site: A0A1V3SGU4_9BURK 
ID   A0A1V3SGU4_9BURK        Unreviewed;       271 AA.
AC   A0A1V3SGU4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Short-chain dehydrogenase {ECO:0000313|EMBL:OOG88239.1};
GN   ORFNames=B0E41_02825 {ECO:0000313|EMBL:OOG88239.1};
OS   Hydrogenophaga sp. A37.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG88239.1, ECO:0000313|Proteomes:UP000189189};
RN   [1] {ECO:0000313|EMBL:OOG88239.1, ECO:0000313|Proteomes:UP000189189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37 {ECO:0000313|EMBL:OOG88239.1,
RC   ECO:0000313|Proteomes:UP000189189};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484, ECO:0000256|RuleBase:RU000363}.
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:OOG88239.1}.
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DR   EMBL; MUNZ01000057; OOG88239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3SGU4; -.
DR   STRING; 1945864.B0E41_02825; -.
DR   OrthoDB; 9797538at2; -.
DR   Proteomes; UP000189189; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189189}.
SQ   SEQUENCE   271 AA;  28945 MW;  9F9E60D49AC5D13D CRC64;
     MNEAHTAGAE RPLVLITGAS SGIGQALALR YAQAGYRLAL VARRSEALQA WVDAQKWDDQ
     RCRVYRADVA ETGSVIEAGE RCLAEQGVPD VVIANAGISI GMDTSERDDV EVMARTFATN
     NTGLAATFHP FVSAMVARGT GRLVGIASVA AIRGLPGHGA YCASKAAVVA YCESLRGELR
     SSGVAVVTLL PGYVDTPLTQ ENRYAMPFLL SPEVFADRAF DTIEAGTSYR VIPWQMGVVA
     KLLRLLPNPL FDRLLAGRAR KHRQGEGRAT G
//
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