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Database: UniProt
Entry: A0A1H0PGP9_9BRAD
LinkDB: A0A1H0PGP9_9BRAD
Original site: A0A1H0PGP9_9BRAD 
ID   A0A1H0PGP9_9BRAD        Unreviewed;       349 AA.
AC   A0A1H0PGP9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=L-idonate 5-dehydrogenase {ECO:0000313|EMBL:SDP04164.1};
GN   ORFNames=SAMN05444050_5680 {ECO:0000313|EMBL:SDP04164.1};
OS   Afipia sp. GAS231.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1882747 {ECO:0000313|EMBL:SDP04164.1, ECO:0000313|Proteomes:UP000198617};
RN   [1] {ECO:0000313|EMBL:SDP04164.1, ECO:0000313|Proteomes:UP000198617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS231 {ECO:0000313|EMBL:SDP04164.1,
RC   ECO:0000313|Proteomes:UP000198617};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; LT629703; SDP04164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0PGP9; -.
DR   STRING; 1882747.SAMN05444050_5680; -.
DR   OrthoDB; 9809185at2; -.
DR   Proteomes; UP000198617; Chromosome i.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08232; idonate-5-DH; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43161; SORBITOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43161:SF9; SORBITOL DEHYDROGENASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198617};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          29..142
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          183..309
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   349 AA;  36194 MW;  9C3BAF38CDC919A9 CRC64;
     MTSMALAATL FGPEDLRMVE RPLDPLASGM VRIRFGAGGI CGSDMHYYRH ARTGDFVVTS
     PLVLGHEISG EVVEIAGAAP GLKIGDRVAV NPSRWCGHCK PCRENRQNLC ENIFFMGSAS
     KTPHMQGGFA SMFDAVPAQC VKIPDHVPYQ AAALAEPLAV CLHAVARAGD VTGKRAVLFG
     AGPIGLLTML AARRAGVADV TVVDIAAAPL AFATRLGANH VVDISGGDEA LKAQAAAQPF
     DVAFEVSGTA AGLASAIGVV RRGGIVVQVG NLPGGQIPVP ANAVMAKEID LRGSFRFGLE
     FFTAVELIAD GSVDVLALVT AQRPLAVAPD AVRLALDRSQ SVKVVLTAQ
//
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