ID V4Q6G8_9CAUL Unreviewed; 317 AA.
AC V4Q6G8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Flavonol synthase {ECO:0000313|EMBL:ESQ93435.1};
GN ORFNames=ABENE_05900 {ECO:0000313|EMBL:ESQ93435.1};
OS Asticcacaulis benevestitus DSM 16100 = ATCC BAA-896.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1121022 {ECO:0000313|EMBL:ESQ93435.1, ECO:0000313|Proteomes:UP000017837};
RN [1] {ECO:0000313|EMBL:ESQ93435.1, ECO:0000313|Proteomes:UP000017837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16100 {ECO:0000313|EMBL:ESQ93435.1,
RC ECO:0000313|Proteomes:UP000017837};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|RuleBase:RU003682}.
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:ESQ93435.1}.
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DR EMBL; AWGB01000008; ESQ93435.1; -; Genomic_DNA.
DR RefSeq; WP_018080497.1; NZ_AWGB01000008.1.
DR AlphaFoldDB; V4Q6G8; -.
DR STRING; 1121022.GCA_000376105_00830; -.
DR PATRIC; fig|1121022.4.peg.1174; -.
DR eggNOG; COG3491; Bacteria.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000017837; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF272; SEXUAL DIFFERENTIATION PROCESS PROTEIN ISP7; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000017837}.
FT DOMAIN 171..276
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 317 AA; 34831 MW; CD40C9D7E8E1D311 CRC64;
MPDTPAPVSA IPPVPLALYE TDFAAFSQSL GAAFERYGFA VLGGHGLDPA LLDRALSATK
AFFALPEATK LRYRQTGMGG ARGYTPFGIE TAKGATHHDL KEFWHIGREL PAGHPYTDYM
PENLWPQEIA DFHASTYALY EALDTLGKKV LRAIATYLKL DAEFFTPTVK DGNSVLRLLH
YPPVTTPGES VRAGAHGDIN VITLLLGAEE PGLQLLDRDG QWLPITPPAD CIVCNIGDML
SRLTNGVLPS TQHRVINPAE GRKDFARYST PFFLHFEPPY VIEILPNCIT PEHPDLGGEP
ITAQDFLMQR LREIKLA
//
