ID Q1GND5_SPHAL Unreviewed; 492 AA.
AC Q1GND5;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 24-JAN-2024, entry version 90.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|ARBA:ARBA00031986};
GN OrderedLocusNames=Sala_3134 {ECO:0000313|EMBL:ABF54837.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF54837.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF54837.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000256|ARBA:ARBA00004829,
CC ECO:0000256|RuleBase:RU362075}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046, ECO:0000256|RuleBase:RU362075}.
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DR EMBL; CP000356; ABF54837.1; -; Genomic_DNA.
DR RefSeq; WP_011543399.1; NC_008048.1.
DR AlphaFoldDB; Q1GND5; -.
DR STRING; 317655.Sala_3134; -.
DR KEGG; sal:Sala_3134; -.
DR eggNOG; COG1233; Bacteria.
DR HOGENOM; CLU_019722_2_1_5; -.
DR OMA; INYPKGG; -.
DR OrthoDB; 9774675at2; -.
DR Proteomes; UP000006578; Chromosome.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:UniProt.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008150; Phytoene_DH_bac_CS.
DR NCBIfam; TIGR02734; crtI_fam; 1.
DR PANTHER; PTHR43734:SF3; B-CAROTENE KETOLASE; 1.
DR PANTHER; PTHR43734; PHYTOENE DESATURASE; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00982; PHYTOENE_DH; 1.
PE 3: Inferred from homology;
KW Carotenoid biosynthesis {ECO:0000256|ARBA:ARBA00022746,
KW ECO:0000256|RuleBase:RU362075};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362075};
KW Reference proteome {ECO:0000313|Proteomes:UP000006578}.
FT DOMAIN 13..490
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 492 AA; 53569 MW; B25AA0C28E613A8A CRC64;
MTRTAIVIGA GFGGLALAIR LQSAGVATTI VEARDKPGGR AYHWVRDGFT FDAGPTVITD
PPCLSDLWEL SGQDMAADVE LMPVSPFYRL NWPDGTNFDY SNDEAALHAE IARLNPADVA
GYERFLDYSK GVYEQGYVKL GATAFLDFRA MIRAAPALMK YQAWRSVYSI VSSYVQDERL
RQALSFHTLL VGGNPMTTSA IYALIHTIEK DGGVWFARGG TNRLVAALIR LFERLGGTLR
LGDAVTAIHT AGDRATGVTT ASGWRGDAEM IACNGDLMHA YRDLLADHPR GPKTARSLAR
KRWSPSLFVV HFGAKGDYPG VAHHSILFGP RYKGLLDDIY KNGVVPDDFS LYLHHPSITD
PGMAPPGHST FYALAPVAHL GKAKADWDGD FGTRFADAII DEVERRVAPD LRANIVTRFH
YTPTDFGRDL NAHLGSAFSL EPVLWQSAFF RAHNRDDRIS NLYFVGAGTH PGAGIPGVVG
SAKATAALML DL
//