ID A4GI67_9BACT Unreviewed; 502 AA.
AC A4GI67;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Phytoene dehydrogenase {ECO:0000256|ARBA:ARBA00031986};
GN ORFNames=ALOHA_HF1029C11.0005 {ECO:0000313|EMBL:ABL97778.1};
OS uncultured marine bacterium HF10_29C11.
OC Bacteria; environmental samples.
OX NCBI_TaxID=415445 {ECO:0000313|EMBL:ABL97778.1};
RN [1] {ECO:0000313|EMBL:ABL97778.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17359257; DOI=10.1111/j.1462-2920.2006.01203.x;
RA McCarren J., Delong E.F.;
RT "Proteorhodopsin photosystem gene clusters exhibit co-evolutionary trends
RT and shared ancestry among diverse marine microbial phyla.";
RL Environ. Microbiol. 9:846-858(2007).
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; EF089401; ABL97778.1; -; Genomic_DNA.
DR AlphaFoldDB; A4GI67; -.
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}.
FT DOMAIN 19..497
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 502 AA; 55973 MW; 019501A09E80085C CRC64;
MAATGNSNRN AAVIGSGFGG LGAAIRLQSA GIQTVLYEAR DLPGGRAYVY HDDGFTFDAG
PTVITAPHVL TDLFDLTDRK LEDYIKLMEV QPMYRLIWSD GDRFDYVRDE ATMVQQIAKR
SQSDAEGYQK FFEYAKKVFH KGYTELADRP FLKFSDMMAV SPALIKLRAD RSVYKTISKY
VKDDHLRQAL SFHSLLVGGN PFQTSSIYTL IHYLEREWGV FFPEGGTHAL VRTLVKLFEE
LGGEIRLSTP VKSVDVLKNG EGNVHRITDG NGAQQDYDMV ISNADVHHTY KKLYSNSKIA
QKRAKKLEKM DWSMSLFVLY FGTDIEYNDV AHHTILFGPR YKELLDEIFK GSKLPDDFSL
YLHVPTVTDK SLAPEGCSAA YVLAPVPHLG RADVDWDSIA EEYGDRIIEA LEVEMPELSK
HIVTRRHITP KTFEDELAAY KGSAFSVAPK LTQSAYFRPS NKDSGIDGLY IVGAGTHPGA
GLPGVLNSAK ATVDLILSEL DN
//